KR20060133558A - Chewing gum comprising biodegradable polymers and having accelerated degradability - Google Patents

Abstract

The invention relates to chewing gum comprising at least one polymer, chewing gum ingredients and enzymes, wherein at least on of said polymers forms a substrate for at least one of said enzymes. According to the invention the degradation of chewing gum comprising a combination of biodegradable polymers and enzymes is accelerated compared to chewing gum without enzymes. By incorporation of enzymes it is possible to obtain a chewing gum, which is relatively fast degrading compared to chewing gum, which is exposed to normal environmental conditions only.

Description

Chewing gum comprising biodegradable polymers and having accelerated degradability

The present invention relates to chewing gums comprising biodegradable polymers and having accelerated degradability.

A chewing gum that has fallen to the floor in an indoor or outdoor environment generally causes significant nuisance and discomfort due to the fact that it is strongly adhered to the surfaces and streets and pavement surfaces and to the shoes and clothing of those who are in or passing through them. It is recognized. In addition to such problems and inconveniences, the fact that currently available chewing gum products are based on the use of natural or artificial elastic and elastomeric polymers which are substantially non-degradable in the environment. Become.

Thus, municipalities and other personnel responsible for the cleanup of indoor and outdoor environments must make considerable efforts to remove chewing gum that has fallen to the floor, but such efforts are expensive and do not produce satisfactory results.

To reduce problems associated with the generalized use of chewing gum, for example, to improve the cleaning method to be more effective in removing chewing gum residues that have fallen to the floor, or to anti-sticking chewing gum formulations. Attempts have been made such as including agents. However, none of these cautions contributed significantly to the solution of the pollution problem.

There has been an increasing interest in synthetic polymers for a variety of applications from biomedical devices to gum bases over the past two decades. Many of these polymers are readily hydrolyzed into their monomeric hydroxy-acids, which are easily removed by metabolic pathways. Biodegradable polymers are an alternative to traditional, non-degradable or low-degradable plastics such as, for example, poly (styrene), poly (isobutylene), and poly (methyl-methacrylate). It is expected.

Thus, recently, for example, in US Pat. No. 5,672,367, chewing gums contain chemically labile bonds that can degrade into water-soluble and non-toxic constituents by the effect of light in the polymer chains or by hydrolysis. It has been disclosed that it can be prepared from some synthetic polymers having. One or more degradable polyesters obtained by the polymerization of cyclic esters based on the claimed chewing gum cyclic esters such as lactides, glycolides, trimethylene carbonate and s-caprolactone Polymers. In this patent application it is mentioned that chewing gum made from polymers called biodegradable is degradable in the environment.

However, a problem associated with the prior art is that even biodegradable chewing gum can inherit unsatisfactory degradation rates in some situations.

It is an object of the present invention to obtain chewing gums having a much faster dissolution rate than those described in the prior art.

The present invention relates to a chewing gum comprising one or more polymers, chewing gum components and enzymes, wherein the one or more such polymers form a substrate for one or more of the enzymes.

According to the present invention, chewing gum polymers that form the substrate of an enzyme may be vulnerable to enzymatic action in that they contain chemical bonds whose degradation is catalyzed by the enzyme. Thus, according to the present invention, degradation of chewing gum comprising a combination of polymers and enzymes can be facilitated as compared to degradation of chewing gum not by enzymes. By the inclusion of enzymes it is possible to obtain chewing gums that are exposed only to normal environmental conditions and degrade relatively quickly compared to chewing gums. Degradation according to the invention results in disintegration of smaller lumps, oligomers, trimers, dimers, and ultimately monomers and smaller products of chewing gum. Bring. Whether the degree of degradation is partial or complete depends on elapsed time, pH, moisture, temperature and other chemical, physical and environmental factors.

In one embodiment of the invention, the chewing gum comprises center filling.

In the preparation of the chewing gum according to the invention, the enzymes are contained in the core and consequently mixed into all parts of the chewing gum during chewing, whereby an enzymatic catalytic effect on degradation can be obtained. Enzymes included can be added, for example, in liquids or powders or encapsulated.

In an embodiment of the invention, the chewing gum comprises a coating.

Thus, the enzymes may be included in the coating of the chewing gum and still produce a substantially desired effect following the chewing gum, and to some extent, one or more of the substrate's available enzyme concentration and substrate, ie the chewing gum. Will result in mixing of the polymers. Against this background, the chewing gum coat, or the core or part of the core, is considered part of the chewing gum, but most applications refer to the chewing gum and the coating as two parts of the tablet.

In one embodiment of the invention, the chewing gum ingredients comprise sweeteners and flavoring agents.

In one embodiment of the invention, the chewing gum ingredients comprise softners and other additives.

In one embodiment of the invention, the at least one polymer constitutes a chewing gum base.

In one embodiment of the invention, the one or more polymers comprise one or more copolymers.

In one embodiment of the invention, the one or more copolymers are polymerized from two or more different monomers, each constituting 1-99%.

Copolymerization provides a polymer with relatively low crystallinity, whereby amorphous regions provide improved resolution.

In one embodiment of the invention, the one or more polymers comprise one or more biodegradable polymers.

In one embodiment of the invention, the chewing gum comprises one or more biodegradable polymers and one or more enzymes.

According to the present invention, chewing gums comprising biodegradable polymers and enzymes exhibit improved degradability.

Application of one or more polymers generally considered biodegradable may increase the effectiveness of the enzymes involved in that the biodegradable polymers may be highly susceptible to enzymatic effects. Some useful biodegradable polymers may be copolymerized from different monomers, the copolymerization encourages amorphous regions and consequently the biodegradable polymers may be much more susceptible to enzymatic attack.

In one embodiment of the invention, the at least one biodegradable polymer comprises at least one biodegradable elastomer.

In one embodiment of the invention, the at least one biodegradable polymer comprises at least one biodegradable elastomeric plasticizer.

In one embodiment of the invention, at least one of the at least one biodegradable polymer comprises at least one polyester obtained by the polymerization of at least one cyclic ester.

Preferably, such polymerization is ring opening polymerization of cyclic esters, which provides aliphatic polyester polymers that are more susceptible to enzymatic degradation than aromatic polyesters. By the polymerization of rings such as lactide, the final degradation product is known as lactic acid which is not harmful to the environment and for some degradation in chewing gum before it is consumed, lactic acid has a positive effect on the taste in fruit-flavored chewing gum. You can have until.

In one embodiment of the invention, at least one of the at least one biodegradable polymer comprises at least one polyester polymer obtained by polymerization of at least one alcohol or derivative thereof and at least one acid or derivative thereof.

In one embodiment of the invention, at least one of said at least one biodegradable polymer is obtained by polymerization of at least one compound selected from the group of cyclic esters, alcohols or derivatives thereof and carboxylic acids or derivatives thereof. At least one polyester.

In one embodiment of the invention, the one or more polyesters obtained by the polymerization of one or more cyclic esters are at least partially derived from α-hydroxy acids such as lactic and glycolic acids.

In one embodiment of the invention, the at least one polyester obtained by the polymerization of at least one cyclic ester is derived from an α-hydroxy acid and the polyester obtained is at least 20 mol% of an α-hydroxy acid units, Preferably at least 50 mol% of α-hydroxy acid units and most preferably at least 80 mol% of α-hydroxy acid units.

In one embodiment of the invention, the one or more cyclic esters are selected from the group of glycolides, lactides, lactones, cyclic carbonates or mixtures thereof.

In one embodiment of the invention, the lactone monomers are selected from the group of ε-caprolactone, δ-valerolactone, γ-butyrolactone, and β-propiolactone. These also include ε-caprolactones substituted with one or more alkyl or aryl substituents at non-carbonyl carbon atoms on the ring, including compounds containing two substituents on the same carbon atom, ? -valerolactones,? -butyrolactones, or? -propiolactones.

In one embodiment of the invention, the carbonate monomer is trimethylene carbonate, 5-alkyl-1,3-dioxan-2-one, 5,5-dialkyl-1,3-dioxan-2- On, or 5-alkyl-5-alkyloxycarbonyl-1,3-dioxan-2-one, ethylene carbonate, 3-ethyl-3-hydroxymethyl, propylene carbonate, trimethylolpropane monocarbon Carbonate, 4,6-dimethyl-1,3-propylene carbonate, 2,2-dimethyl trimethylene carbonate, and 1,3-dioxepan-2-one and mixtures thereof.

In one embodiment of the invention, the cyclic ester polymers and their copolymers resulting from the polymerization of the cyclic ester monomers are poly (L-lactide); Poly (D-lactide); Poly (D, L-lactide); Poly (methoractide); Poly (glycolide); Poly (trimethylene carbonate); Poly (epsilon-caprolactone); Poly (L-lactide-co-D, L-lactide); Poly (L-lactide-co-meso-lactide); Poly (L-lactide-co-glycolide); Poly (L-lactide-co-trimethylenecarbonate); Poly (L-lactide-co-epsilon-caprolactone); Poly (D, L-lactide-co-meso-lactide); Poly (D, L-lactide-co-glycolide); Poly (D, L-lactide-co-trimethylenecarbonate); Poly (D, L-lactide-co-epsilon-caprolactone); Poly (meth-lactide-co-glycolide); Poly (metho-lactide-co-trimethylenecarbonate); Poly (metho-lactide-co-epsilon-caprolactone); Poly (glycolide-co-trimethylenecarbonate); Poly (glycolide-co-epsilon-caprolactone).

In one embodiment of the invention, the at least one polymer has a crystallinity in the range of 0 to 95%, more preferably in the range of 0 to 70%.

Preferably, a polymer having low-crystallinity regions is due to the fact that the decomposition catalyzed by the chewing gum enzyme according to the invention can occur more easily in polymer regions with lower crystallinity than those with higher crystallinity. Include them. In some cases, degradation by enzymes may degrade the amorphous regions and the polymer may be partially degraded leaving only crystalline regions.

In one embodiment of the invention, one or more of the one or more polymers have amorphous regions.

In one embodiment of the invention, said at least one polymer is aliphatic.

In one embodiment of the invention, the molecular weight of said at least one polymer is in the range of 500-500000 g / mol, preferably in the range of 1500-200000 g / mol Mn.

In one embodiment of the invention, one or more of the enzymes catalyze the degradation of the one or more polymers.

In one embodiment of the invention, the chewing gum after use is partially disintegrated due to the effects of the enzymes.

The remaining chewing gum mass after use can change its structure due to enzymatic effects, and experiments have shown that if some conditions are met, the chewing gum mass is separated from the surfaces to which the mass is attached. In other words, non-tack can be obtained without visual decomposition of the mass.

In one embodiment of the invention, one or more of the enzymes affects the polymer substrate, resulting in partial disintegration of the chewing gum.

In one embodiment of the invention, one or more of the enzymes affects the polymer substrate resulting in partial disintegration and crumbling structure of the chewing gum.

The remaining chewing gum mass after use is partially decomposed due to the enzymatic catalyst, whereby the remaining portions are outdoors, for example by environmental factors such as weather conditions such as rainfall and brush or vacuum cleaners. It can be easily removed indoors by physical factors.

In one embodiment of the invention, after use of the chewing gum one or more of the enzymes catalyze polymer matrix degradation until the one or more polymers are completely degraded.

Once fully degraded, polymer residues are the basic compounds that can enter the natural circulation.

In one embodiment of the invention, one or more of the enzymes are active under the atmosphere and at their pressure and promote degradation of the one or more polymers.

The natural outdoor environment is an important factor in the degradation by enzymes. Enzyme activity should be optimal under atmospheric conditions.

In one embodiment of the invention, one or more of the enzymes are included in chewing gum, gum base, center filling or coating.

According to the invention, the enzymes can be placed in one of the chewing gum moieties and still provide for accelerated degradation following mixing of the enzyme and polymer substrate during chewing.

In one embodiment of the invention, one or more of the enzymes facilitate the degradation of the polyester obtained by ring-open polymerization of one or more cyclic esters.

In one embodiment of the invention, one or more of the enzymes facilitate the degradation of the polyester obtained by the polymerization of one or more alcohols or derivatives thereof and one or more acids or derivatives thereof.

Studies have shown that polyesters in these two polyester groups are particularly vulnerable to the catalytic effects on their degradation. Thus, the application of these polymers in enzyme-containing chewing gum can provide chewing gum that is particularly degradable.

In one embodiment of the invention, the chewing gum is obtained by ring opening polymerization of one or more polyesters and one or more cyclic esters obtained by polymerization of one or more alcohols or derivatives thereof and one or more acids or derivatives thereof. At least one polyester.

In one embodiment of the invention, the chewing gum has a moisture content of less than 10% by weight, preferably less than 5% by weight, more preferably less than 1% by weight and most preferably less than 0.1% by weight.

Unless chewing gum is used, it is important to keep the moisture content low to protect the chewing gum from degradation, for example hydrolysis by hydrolases.

In one embodiment of the invention, the chewing gum is at least 0.1% by weight, preferably at least 5% by weight, more preferably at least 10% by weight, even more preferably at least 20% by weight and most preferably at least 40% by weight. It can absorb a large amount of moisture.

When moisture is absorbed into the chewing gum, the conditions for hydrolysis to occur are improved. Water absorption is an important parameter for controlling the degradability of biodegradable chewing gum. This is particularly important when the enzymes applied are hydrolases.

In one embodiment of the invention, the chewing gum comprises filler in an amount of 0 to 80% by weight.

The filler content may provide the chewing gum with higher water absorption and thus more favorable conditions for degradation, eg hydrolysis and oxidation, which are catalyzed by enzymes.

In one embodiment of the invention, the concentration of the enzyme is in the range of 0.001% to 50% by weight of the chewing gum.

Higher enzyme concentrations result in more degradation in terms of speed and completeness. In addition, higher concentrations are more likely to result in increased concentrations of enzymes in chewed chewing gum. However, if the enzyme concentration is too high, degradation by the enzyme may be hindered.

In one embodiment of the invention, the concentration of the enzyme is in the range of 0.001% to 10% by weight of the chewing gum.

In one embodiment of the invention, the concentration of the enzyme is in the range of 0.01% to 5% by weight of the chewing gum.

In one embodiment of the invention, the amount of the enzyme is in the range of 0.0001 to 80% by weight relative to the amount of the gum base of the chewing gum.

In one embodiment of the invention, the amount of the enzyme is in the range of 0.001 to 40% by weight relative to the amount of the gum base of the chewing gum.

In one embodiment of the invention, the amount of the enzyme is in the range of 0.1 to 20% by weight relative to the amount of the gum base of the chewing gum.

In one embodiment of the invention, one or more of the enzymes are oxidoreductases, transferases, hydrolases, lyases, isomerases And ligases.

In one embodiment of the invention, one or more of the enzymes are oxidoreductases.

In one embodiment of the invention, one or more of the enzymes is a hydrolase.

In one embodiment of the invention, one or more of the enzymes is a lyase.

In one embodiment of the invention, one or more of the hydrolases act on ester bonds.

In one embodiment of the invention, the at least one hydrolase is a glycosylase.

In one embodiment of the invention, one or more of the hydrolases act on ether bonds.

In one embodiment of the invention, one or more of the hydrolases act on carbon-nitrogen bonds.

In one embodiment of the invention, one or more of the hydrolases act on peptide bonds.

In one embodiment of the invention, one or more of the hydrolases act on acid anhydrides.

In one embodiment of the invention, at least one said hydrolase acts on carbon-carbon bonds.

In one embodiment of the invention, one or more of the hydrolases are halide bonds, phosphorus-nitrogen bonds, sulfur-nitrogen bonds, carbon-phosphorus bonds, sulfur-sulfur bonds or carbon-sulfur Act on the bonds.

In one embodiment of the invention, at least one of the enzymes is selected from the group of lipases, esterases, depolymerases, peptidases and proteases.

Because of the polymer properties of the substrates according to the invention, enzymes such as different dipolymerases are suitable for their degradation since they have the ability to catalyze the decomposition of different polymer types. In addition, lipases can be used for polymer degradation since they can degrade the bonds found in oil and solid phases. For some preferred polymers comprising ester linkages, the most convenient enzymes can generally be classified into the group of esterases. Likewise, peptidases and proteases have been found to degrade various polymer substrates.

In one embodiment of the invention, one or more of the enzymes is an endo-enzyme.

In one embodiment of the invention, one or more of the enzymes is an exo-enzyme.

In one embodiment of the invention, one or more of the enzymes have a molecular weight of 2 to 1000 kDa, preferably 10 to 500 kDa.

In one embodiment of the invention, two or more of the enzymes are combined.

In the present invention, a combination of two or more enzymes means that these enzymes are added to the same chewing gum. By addition of two or more different kinds of enzymes, for example two different hydrolases, or for example hydrolases and oxidases in the same chewing gum, the enzymatic effect on degradation is significantly improved. Can be.

In one embodiment of the invention, one or more of the enzymes require a co-factor to perform the catalytic function.

In one embodiment of the invention, one or more of the enzymes are included in the chewing gum.

In one embodiment of the invention, one or more of the enzymes is included in the gum base. In one embodiment of the invention, one or more of the enzymes are included in the coating.

By environmental factors in nature, degradation proceeds primarily on the surfaces of the polymer, for example, but by incorporating enzymes into the chewing gum, degradation proceeds from within, whereby the disintegration of the gum is more likely to occur during degradation. Can be started at an early stage.

In one embodiment of the invention, one or more of the enzymes have an optimal activity in the pH range of 1.0 to 11.0, preferably in the pH range of 4.0 to 8.0, and most preferably in the pH range of 4.0 to 6.0.

In one embodiment of the invention, one or more of the enzymes are at temperatures in the range of -10 to 60 ° C, preferably 0 to 50 ° C, more preferably 5 to 40 ° C, and most preferably 10 to 35 ° C. Have optimal activity.

In one embodiment of the invention, one or more of the enzymes have an optimum activity at relative humidity in the range of 10 to 100% RH, preferably 30 to 100% RH.

Preferably, the enzymatic effect on the degradation of the chewing gum polymer of the enzymes is significant under the chemical and physical conditions typically found in the natural environment in which the chewing gum can be placed.

In one embodiment of the invention, the chewing gum is prepared by a one-step process.

In one embodiment of the invention, the chewing gum is prepared by a two-step method.

In one embodiment of the present invention, the chewing gum is prepared by a continuous mixing process.

In one embodiment of the invention, the chewing gum is compressed and manufactured by the use of compression techniques.

The invention also relates to the use of one or more enzymes for the degradation of biodegradable chewing gum.

In one embodiment of the invention, the one or more enzymes comprise hydrolases.

The invention also relates to one or more biodegradable polymers that are at least partially degraded by one or more enzymes.

In one embodiment of the invention, the enzyme is mixed with the one or more biodegradable polymers by chewing.

The present invention relates to chewing gum comprising biodegradable polymers, chewing gum components and enzymes. By such means, a chewing gum can be provided in which the polymers make up the substrates for the enzymes and consequently partially degrade.

According to the present invention, biodegradable polymers in chewing gum can be degraded by enzymes, which can lead to increased polymer degradation in rate and degree of degradation compared to non-enzymatic degradation. .

The use of enzymes for the purpose of degradation of chewing gum polymers can be considered to have limited biodegradability under normal circumstances and can advantageously promote the possibility of including polymers to some extent avoided in biodegradable chewing gum compositions. The beneficial effect on the desired texture that these polymers may have can be obtained due to the use of enzymes without compromising the degradability of the chewing gum.

In an embodiment of the invention, degradation of the biodegradable polymer may be improved and / or promoted when applied under environmental conditions that will not occur untriggered.

When chewing gum is processed on land in outdoor environments, there are a number of chemical, physical and biological factors, which facilitate the degradation of biodegradable polymers. However, if, for example, it falls on a pavement or indoors, it may not be able to encounter the situations required for the chewing gum disassembly. In such cases, even biodegradable chewing gum can be inconvenient. The solution according to the invention can facilitate the acceleration of decomposition in environments where conditions only degrade very weakly. The presence of enzymes allows the degradation process to proceed faster than if the only influences in the environment were physical and / or chemical factors.

According to a preferred definition of biodegradability according to the present invention, biodegradability is simpler compounds, in combination with chemical processes such as hydrolysis, often through enzymatic or microbiological methods when exposed to the natural environment or placed in a living organism. And ultimately the nature of some organic molecules that react to form carbon dioxide, nitrogen oxides, methane, water and their equivalents.

As used herein, the term 'biodegradable polymers' refers to polymer compounds that are environmentally or biologically degradable and are discarded by chewing gum and then discarded by physical, chemical, and / or biological degradation. It refers to chewing gum base components that allow the gum to be more easily removed from the waste site or ultimately disintegrate into chunks or particles that are no longer recognized as chewing gum residue. Degradation or disintegration of such degradable polymers may involve physical factors such as temperature, light, moisture, etc., chemical factors such as oxidative conditions, pH, hydrolysis, or biological factors such as microorganisms and / or enzymes. It may be carried out or derived by. The degradation products may be larger oligomers, trimers, dimers and monomers.

Preferably, the final decomposition products are small inorganic compounds such as carbon dioxide, nitrogen oxides, methane, ammonia, water and the like.

In some useful embodiments, all polymer components of the gum base are polymers that can be environmentally or biologically degraded.

As used herein, the term 'enzyme' is used in the same sense as used within biochemistry and molecular biology. Enzymes are biological catalysts, typically proteins or non-proteins with enzymatic properties have also been found. Enzymes are derived from living individuals, which act as catalysts to regulate the rate at which chemical reactions progress without changing themselves in the process. The biological processes that occur in all living individuals are chemical processes, and enzymes regulate most of them. Without enzymes, many of these reactions would not occur at an appreciable rate. Enzymes catalyze all aspects of cell metabolism. This includes the conservation and conversion of chemical energy, the construction of cellular macromolecules from smaller precursors and the digestion of foods, where large nutrient molecules such as proteins, carbohydrates and fats are broken down into smaller molecules.

In general, enzymes have useful industrial and medical applications. Wine fermentation, bread fermentation, cheese curling and beer brewing have been carried out at the earliest, but it was not until the nineteenth century that such reactions were the result of the catalytic activity of enzymes. Since then, enzymes have been of increasing importance in industrial processes involving organic chemical reactions. Research and development of enzymes is still ongoing and new applications of enzymes are being discovered. Theories have been proposed to explain this phenomenon that synthetic polymers are hardly degraded by enzymes and enzymes attack chain ends and the chain ends of artificial polymers are deep within the polymer matrix. However, experiments according to the present invention have surprisingly shown that the effect of adding enzymes to chewing gum is to degrade more polymers of chewing gum.

As a catalyst, enzymes can generally increase the rate of arrival of equilibrium between reactants and products of chemical reactions. According to the invention, these reactants comprise different degrading substances such as polymers and water, oxygen or other reactive substances which are present adjacent to the polymers, whereas the products are oligomers, trimers Retention, dimers, monomers and smaller decomposition products. When the reactions are catalyzed by an enzyme, one or more reactants form a substrate for one or more enzymes, which means that a transient bond between the reactants, ie, enzyme substrates and enzymes, appears. In different ways, for example, by bringing the reactants into structures or positions that favor the reaction, this binding allows the reaction to proceed faster. Increasing the rate of reaction due to enzymatic effects, i.e. catalysis, generally occurs because it lowers the activation energy barrier for the reaction to occur. However, since the presence of the catalyst does not affect the position of the equilibrium, the enzymes do not change the difference in free energy levels between the initial and final states of the reactants and products. At the end of the catalytic reaction, one or more enzymes release the product or products and return to their original state, ready for another substrate.

Temporal binding of one or more substrate molecules occurs in regions of the enzyme called active sites and may include, for example, hydrogen bonding, ionic interactions, hydrophobic interactions or weak covalent bonds. In the complex tertiary structure of enzymes, the active sites take the form of pockets or clefts, which fit into specific substrates or portions of substrates. Some enzymes have very specific modes of action, while others have broad specificity and can catalyze a series of different substrates. Basically, molecular structures are important for the specificity of enzymes and they can be made active or inactive by changing pH, temperature, solvents and the like. However, some enzymes require co-enzymes or other co-factors to take effect, and in some cases co-enzymes form association complexes that act as donors or receptors for specific functional groups. do. Occasionally, enzymes may be specified as endo-enzymes or exo-enzymes, depending on the mode of action. According to this term, exo-enzymes attack the chain ends of polymer molecules and thereby release terminal residues or single units, for example, while endo-enzymes attack the mid-chain and It acts on internal bonds inside polymer molecules, breaking up larger molecules into smaller molecules. In general, enzymes can be obtained in liquids or powders and ultimately encapsulated in a variety of materials.

Today, thousands of different enzymes have been discovered and more enzymes have been discovered, so the number of known enzymes is still increasing. For this reason, the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) has established a reasonable naming and numbering system. In this specification, enzyme names are used in accordance with the recommendations devised by NC-IUBMB.

In the following the general principles for making embodiments according to the invention are described together with the general description of the products obtained.

Two fairly different aspects of the present invention are briefly summarized. A first aspect according to one embodiment of the present invention is to address the possibility of increasing the degradability of a biodegradable chewing gum applied in a chewing gum having only a polymer matrix or partially comprising biodegradable polymers. A second, significantly different aspect is to facilitate the use of conventional polymers or biodegradable polymers without catalytic enzymes, for example, less suitable for their application in terms of degradation rate.

In summary, they and additional aspects are obtained by applying enzymes as degradation triggers and catalysts in chewing gum. In other words, according to the present invention, one or more biodegradable polymers of chewing gum form a substrate paired with a suitable enzyme. Several different criteria should be considered when determining which enzymes should be matched by which polymers and by what processes.

According to four preferred embodiments of the invention, the enzyme-containing biodegradable chewing gum is a conventional two-stage batch method, a less used but highly promising one-stage method or continuous mixing performed by an extruder, for example. And a fourth preferred embodiment is the manufacture of chewing gum by the use of compression techniques.

The two-step method includes a separate preparation step of the gum base and subsequent mixing of the gum base with additional chewing gum components. Several other methods can also be applied. Examples of two-step methods are well described in the prior art. An example of a one-step method is hereby disclosed in WO 02/076229 Al, incorporated herein by reference. Examples of continuous mixing methods are thereby disclosed in US 6 017 565 A, US 5 976 581 A and US 4 968 511 A, incorporated herein by reference. Examples of methods of making a compressed chewing gum are hereby incorporated by reference in US 4405647, US 4753805, WO 8603967, EP 513978, US 5866179, WO / 97/21424, EP 0 890 358, DE 19751330, US 6,322,828. , PCT / DK03 / 00070, PCT / DK03 / 00465.

Where a two-step method is applied, care should be taken, for example to prevent excessive heating of the applied enzymes. This can be done, for example, by mixing the applied enzyme (s) to the chewing gum in a second step, ie, the gum base is mixed with the chewing gum components.

Although the one-step method appears to be quite suitable for its purpose in many respects, when the one-step method is applied, the same problem can be observed, and in some methods temperature control or cooling can be virtually avoided.

If a continuous mixing method is applied, again, active cooling and heating must be carefully controlled to prevent the aforementioned destruction or damage of the applied enzyme (s).

In one of several major embodiments of the invention the chewing gum will be described in more general terms.

Above all, chewing gums include polymer compositions, based in part or wholly on biodegradable polymers. As in the case of conventional non-degradable chewing gums, these polymers are components of chewing gum that provide the texture and "masticatory" properties of chewing gum. Lists of suitable and preferred polymers according to the invention are described below (end of detailed description).

The chewing gum further comprises additives which are applied to obtain the desired fine-tuning of the chewing gum described above. Such additives may include, for example, softeners, emulsifiers, and the like. A list of such suitable and preferred additives is described below (at the end of the detailed description).

In addition, the chewing gum further comprises ingredients adapted to obtain the desired flavor and properties of the chewing gum described above. Such ingredients may include, for example, sweeteners, spices, acids and the like. Lists of such suitable and preferred components are described below (end of detailed description).

It should be emphasized that the additives and components described above may functionally interact. By way of example, the spice can be applied as a softener or act as a softener, for example in a complete system. The strict division between additives and components cannot usually be established.

In addition, a coating may be applied for complete or partial encapsulation of the chewing gum center obtained. In this specification, the coating and core are considered as one whole, and therefore, the term "chewing gum" includes both chewing gum bodies and optional coatings. Examples of different coatings are described below (end of detailed description).

Advantages according to the invention are that partial disintegration or non-tack improvement of the chewing gum mass can be obtained. Further explanation of the advantages is given in two separate examples. One example is when enzymatic effects result in partial disintegration and brittle structure of the mass so that the components forming the mass are released from the surface. Another example deals with the situation in which the chewing gum chunks change their structure due to enzymatic effects, and experiments show that when some conditions are met, the chewing gum chunks are released from the surface to which they are attached. In other words, this non-tacky property can be obtained without visual disintegration of the mass.

It is a further advantage according to the invention that complete dissolution can be obtained, which means that the polymer residues can enter the circulation system in nature. Inclusion of enzymatic effects results in chewing gum polymers that can be fully biodegradable.

According to general principles for the preparation of the embodiments according to the invention, suitable examples of polymers, enzymes and chewing gum components are outlined below.

Suitable examples of environmentally or biologically degradable chewing gum base polymers that can be applied in combination with the gum base of the present invention are degradable polyesters, poly (ester-carbonates), polycarbonates, polyesters Proteins including amides, polypeptides, homopolymers of amino acids such as polylysine, and derivatives thereof such as protein hydrolysates including zein hydrolysates. Particularly useful compounds of this kind are obtained by the polymerization of one or more cyclic esters such as lactide, glycolide, trimethylene carbonate, δ-valerolactone, β-propiolactone and ε-caprolactone Polyester polymers and polyesters obtained by polycondensation of a mixture of open chain polyacids and polyols such as adipic acid and di (ethylene glycol). Hydroxy carboxylic acids, such as 6-hydroxycaproic acid, can also be used to form polyesters or together with mixtures of polyacids and polyols. Such degradable polymers may be homopolymers, copolymers, or terpolymers, including graft-and block-polymers.

Particularly useful biodegradable polyester compounds produced from cyclic esters can be obtained by ring-opening polymerization of one or more cyclic esters, including glycolides, lactides, lactones and carbonates have. The polymerization process can occur in the presence of one or more suitable catalysts, such as metal catalysts, in which octynostannic octoate is a non-limiting example, and the polymerization process can be carried out in polyols, polyamines or a plurality of hydroxyls or other It may be initiated by initiators such as other molecules having reactive functional groups and mixtures thereof.

Thus, particularly useful biodegradable polyesters produced through the reaction of one or more alcohols or derivatives thereof and one or more acids or derivatives thereof are generally di-, tri- or higher functional alcohols or esters thereof. And aliphatic or aromatic carboxylic acids or their esters of di-, tri-, or more functional groups, by means of step-growth polymerization. Similarly, also hydroxy acids or anhydrides and halides of polyfunctional carboxylic acids can be used as monomers. Polymerization includes direct polyesterization or transesterification and can be catalyzed. The use of branched monomers inhibits the crystallinity of the polyester polymers. Mixing of dissimilar monomer units in the chain also inhibits crystallinity. In order to control the reaction and molecular weight of the resulting polymer, the polymer chains are subjected to stoichiometric imbalance by addition of monofunctional alcohols or acids and / or between acid groups and alcohol groups or derivatives thereof. May be terminated for use. In addition, addition of long chain aliphatic carboxylic acids or aromatic monocarboxylic acids can be used to control the degree of branching in the polymer, while polyfunctional monomers are often used for branching. In addition, after polymerization, monofunctional compounds can be used to endcap free hydroxyl and carboxyl groups.

In addition, polyfunctional carboxylic acids are generally high-melting solids with very limited solubility in the polycondensation reaction medium. Often, esters or anhydrides of polyfunctional carboxylic acids are used to overcome this limitation. Polycondensations, including carboxylic acids or anhydrides, produce water as condensate and require high temperatures to remove it. Thus, polycondensations involving transesterification of esters of polyfunctional acids are often the preferred method. For example, dimethyl ester of terephthalic acid can be used in place of terephthalic acid itself. In this case, methanol, not water, is condensed, and methanol can be removed more easily than water. Typically, the reaction is carried out in bulk (without solvent) and high temperatures and vacuum conditions are used to remove by-products and allow the reaction to proceed completely. In addition to esters or anhydrides, halides of carboxylic acids may also be used under certain circumstances.

In addition, for the production of polyesters of this kind, the desired polyfunctional carboxylic acids or derivatives thereof are usually saturated or unsaturated aliphatic or aromatic and have 2 to 100 carbon atoms, more preferably 4 to 18 carbon atoms. Include them. Some applicable examples of carboxylic acids, which can be employed in the polymerization of polyesters of this kind, as such or as derivatives thereof, are oxalic acid, malonic acid, citric acid, succinic acid, malic acid, tartaric acid, fumaric acid, maleic acid, glutaric acid. Aliphatic polyfunctional carboxylic acids and cyclopropane dicarboxylic acid, cyclobutane dicarboxylic acid, cyclohexane dicycloacid, such as acid, glutamic acid, adipic acid, glucaric acid, pimelic acid, suberic acid, azelaic acid, sebacic acid, dodecanedioic acid, etc. Cyclic aliphatic polyfunctional carboxylic acids such as carboxylic acid and aromatic polyfunctional carboxylic acids such as terephthalic acid, isophthalic acid, phthalic acid, trimellitic acid, pyromellitic acid and naphthalene 1,4-, 2,3-, 2,6-dicarboxylic acid And equivalents thereof. For illustrative and non-limiting purposes, some examples of carboxylic acid derivatives are hydroxy acids such as 3-hydroxy propionic acid and 6-hydroxycaproic acid and dimethyl or diethyl esters corresponding to the acids already described above, ie Dimethyl or diethyl oxalic acid, malonic acid, succinic acid, fumaric acid, maleic acid, glutaric acid, adifuic acid, pimelic acid, suberic acid, azelic acid, sebacic acid, dodecanedioic acid, terphthalic acid, isophthalic acid, phthalic acid And anhydrides, halides or esters of acids, meaning esters of acids such as and the like. In general, methyl esters are sometimes preferred over ethyl esters because higher boiling alcohols are more difficult to remove than lower boiling alcohols.

In addition, generally preferred polyfunctional alcohols include 2 to 100 carbon atoms, for example polyglycols and polyglycerols. Some applicable examples of alcohols, which can be employed in the course of polymerization of this kind of polyester, as such or as derivatives thereof, are ethylene glycol, 1,2-propanediol, 1,3-propanediol, 1, 3-butanediol, 1,4-butanediol, 1,6-hexanediol, diethylene glycol, 1,4-cyclohexanediol, 1,4-cyclohexanedimethanol, neopentyl glycol, glycerol, trimethylolpropane, pentaeryt Polyols such as lititol, sorbitol, mannitol and the like. For illustrative and non-limiting purposes, some examples of alcohol derivatives include triacetin, glycerol palmitate, glycerol sebacate, glycerol adipate, tripropionine, and the like.

In addition, for the polymerization of polyesters of this kind, the chain stoppers used sometimes are monofunctional compounds. They are preferably monohydroxy alcohols containing 1-20 carbon atoms or monocarboxylic acids containing 2-26 carbon atoms. General examples are medium-chain or long-chain fatty alcohols or acids, and specific examples are methanol, ethanol, butanol, hexanol, octanol, and the like and lauryl alcohol, myristyl alcohol, cetyl alcohol, ste Monohydroxy alcohols such as aryl alcohol, stearic alcohol, and acetic acid, lauric acid, myristic acid, palmitic acid, stearic acid, arachidic acid, seric acid, dodecylene acid, palmitoleic acid, oleic acid, linoleic acid Monocarboxylic acids such as linolenic acid, erucic acid, benzoic acid, naphthoic acids and substituted naphthoic acids, 1-methyl-2-naphthoic acid and 2-isopropyl-1-naphthoic acid and the like.

In addition, acid catalysts or transesterification catalysts are commonly used in the polymerization of polyesters of this kind and their non-limiting examples are acetates of manganese, zinc, calcium, cobalt or magnesium, and antimony (III) Metal catalysts such as oxides, germanium oxides or germanium halides and tetraalkoxygermanium, titanium alkoxides, zinc or aluminum salts.

Suitable enzymes according to the general principles in the preparation of embodiments which fall within the scope of the invention can be seen to belong to six classes according to their function: oxidoreductases, transferases, hydrolases, Lyases, isomerases and ligases. Oxidoreductases catalyze oxidation-reduction reactions and the substrate to be oxidized is considered a hydrogen or electron donor. Transferases catalyze the transfer of functional groups from one molecule to another. Hydrolases catalyze the cleavage by hydrolysis of various bonds. Lyases catalyze the decomposition of various bonds by means other than hydrolysis or oxidation, for example, these enzymes may be used to remove one functional group from a double bond or to add a single functional group to a double bond, or It is meant to catalyze other cleavages, including rearrangement. Isomerases catalyze intramolecular rearrangement, meaning changes in one molecule. Ligases catalyze reactions in which two molecules are linked.

Some preferred enzymes according to the invention are CH—OH groups, aldehyde or oxo groups, CH—CH groups, CH—NH groups, CH—NH ₂ groups, NADH or NADPH, nitrogenous compounds, sulfur Different groups of donors such as groups, heme groups, diphenols and related substances, single donors containing oxygen molecules, paired donors with inclusion or reduction of oxygen molecules or otherwise Are oxidoreductases.

Oxidoreductases can also act on XH and YH to form CH ₂ groups or XY bonds. Generally, enzymes belonging to oxidoreductases may be referred to as oxidases, oxygenases, hydrogenases, dehydrogenases, reductases, and the like.

Specific examples of oxidoreductases include maleate oxidase, glucose oxidase, hexose oxidase, aryl-alcohol oxidase, alcohol oxidase, long-chain alcohol oxidase, glycerol-3-phosphate oxidase, polyvinyl-alcohol oxidase, D-arabino Os-1.4-lactone oxidase, D-mannitol oxidase, xylitol oxidase, oxalate oxidase, carbon monoxide oxidase, 4-hydroxyphenylpyruvate oxidase, dihydrouracil oxidase, ethanolamine oxidase, L-aspartate oxidase, sarcosine oxidase , Urate oxidase, methanethiol oxidase, 3-hydroxyanthranilate oxidase, laccase, catalase, fatty acid peroxidase, peroxidase, diarylpropane peroxidase, peroxidase, ferroxidase, Putridine Oxidases such as oxidase, columbamine oxidase and equivalents thereof.

Further specific examples of oxidoreductases include catechol 1,2-deoxygenase, gentisate 1,2-deoxygenase, homogenate 1,2-deoxygenase, lipoxygenase, ascorbate 2,3 -Dioxygenase, 3-carboxyethylcatechol 2,3-dioxygenase, indole 2,3-dioxygenase, capate 3,4-dioxygenase, arachidonate 5-lipoxygenase, biphenyl- 2,3-diol 1,2-dioxygenase, linoleate 11-lipoxygenase, acetylacetone-cleaving enzyme, lactate 2-monooxygenase, phenylalanine 2-monooxygenase, inositol Oxygenases such as oxygenase and the like.

Further specific examples of oxidoreductases include alcohol dehydrogenase, glycerol dehydrogenase, propanediol-phosphate dehydrogenase, L-lactate dehydrogenase, D-lactate dehydrogenase, glycerate Dehydrogenase, glucose 1-dehydrogenase, galactose 1-dehydrogenase, allyl-alcohol dehydrogenase, 4-hydroxybutyrate dehydrogenase, octanol dehydrogenane, aryl-alcohol di Hydrogenase, cyclopentanol dehydrogenase, long-chain-3-hydroxyacyl-CoA dehydrogenase, L-lactate dehydrogenase, D-lactate dehydrogenase, butanal dihydro azepin dehydrogenase, terephthalate 1,2-cis-dihydro-diol dehydrogenase, succinate dehydrogenase, glutamate dehydrogenase, glycine-dihydro crab And a dehydratase, hydrogen dehydrogenase, 4-cresol dehydrogenase, phosphonate dehydrogenase and a dehydrogenase acids, such as their equivalents.

Specific examples of reductases belonging to the group of oxidoreductases include diethyl 2-methyl-3-oxosuccinate reductase, trophin reductase, long-chain fatty acid-acyl-CoA reductase, carr Enzymes such as carboxylate reductase, D-proline reductase, glycine reductase, and equivalents thereof.

Other preferred enzymes according to the invention are lyases which may belong to one of the following groups: carbon-carbon lyases, carbon-oxygen lyases, carbon-nitrogen lyases, carbon-sulfur lyases, carbon-halide lyases , Phosphorus-oxygen lyases and other lyases.

Carbon-carbon lyases include carboxy-lyases, aldehyde-lyases, oxo-acid lyases and the like. Some specific examples belonging to the groups include oxalate decarboxylase, acetolactate decarboxylase, aspartate 4-dicarboxylase, lysine decarboxylase, aromatic-L-amino acid dicar Carboxylase, methylmalonyl-CoA decarboxylase, carnitine decarboxylase, indole-3-glycerol-phosphate synthase, gallate decarboxylase, branching -Chain-3-oxoacid decarboxylase, tartarate decarboxylase, arylmalonate decarboxylase, fructose-biphosphate aldolase , 2-dihydro-3-dioxy-phosphogluconate aldolase, trimethylamine-oxide aldolase, propioin synthase, lactate aldolase, vanillin synthase, isocitrate lyase, hydride Roxymethylglutaryl-Co A lyase, 3-hydroxyaspartate aldolase, tryptopanase, deoxyribodipyrimidine photo-lyase, octadecanal dicarbonylase and equivalents thereof.

Carbon-oxygen lyases include lyases that act on hydro-lyases, polysaccharides, phosphates and others. Some specific examples include carbonate dehydratase, fumarate hydratase, aconitate hydratase, citrate dihydratase, arabinate dihydratase, galactonate dihydratase , Altronate dihydratase, mannonate dihydratase, dihydroxy acid dihydratase, 3-dihydroquinate dihydratase, propanediol dihydratase, glycerol dihydratase, Mali Eight hydratase, oleate hydratase, pectate lyase, poly (β-D-manneuronate) lyase, oligogalacturonide lyase, poly (α-L-guluronate) lyase, xantase, ethanol Amine-phosphate phospho-lyase, carboxymethyloxysuccinate lyase and the like.

Examples of the carbon-nitrogen lyases include lyases and amine-lyases that act on ammonia-lyases, amides, amidines, and the like. Specific examples of this group of lyases include aspartate ammonia-lyase, phenylalanine ammonia-lyase, ethanolamine ammonia-lyase, glucosamine ammonia-lyase, argininosuccinate lyase, adenillosuccinate lyase, ureido Glycolate lyase, 3-ketovalideoxylamine CN-lyase.

Carbon-sulfur lyases include some specific examples such as dimethylpropiotetin dithiomethylase, aliin lyase, lactoylglutathione lyase and cysteine lyase.

There are some specific examples of carbon-halide lyases such as 3-chloro-D-alanine dihydrochlorinase or dichloromethane dihalogenase.

Phosphorous-oxygen lyases include some specific examples such as adenylate cyclase, cytidylate cyclase, glycosylphosphatidylinositol diacylglycerol-lyase.

In the most preferred embodiments of the present invention, the enzymes applied are hydrolases, including glycosylases, enzymes and ester bonds acting on acid anhydrides, ether bonds, carbon-nitrogen bonds, peptides Enzymes that act on bonds, carbon-carbon bonds, halide bonds, phosphorus-nitrogen bonds, sulfur-nitrogen bonds, carbon-phosphorus bonds, sulfur-sulfur bonds or carbon-sulfur bonds.

Preferred enzymes among the glycosylases are glycosidases capable of hydrolyzing O- and S-glycol compounds or N-glycosyl compounds. Some examples of glycosylases include α-amylase, β-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3 (4) -β-glucanase, inulinase, endo- 1,4-β-xylanase, oligo-1,6-glucosidase, dextranase, chitinase, polygalacturonase, lysozyme, lebanase, quercitrinase ), Galacturan 1,4-α-galacturonidase, isoamylase, glucan 1,6-α-glucosidase, glucan endo-1,2-β-glucosidase, rickenase, agara Kinase, exo-poly-α-galacturonosidase, κ-carrageenase, steryl-β-glucosidase, strcitosidine β-glucosidase, mannosyl-oligosaccharides Glucosidase, Lactase, Oligoxiglucan β-glycosidase, Polymanneuronate Hydrolase, Chitosanase, Poly (ADP-Ribose) Glycohydrolol Ajay, a purine, such as Leo nyugeul Let Ajay, Ajay Let inosine nucleoside, uridine nucleoside Let kinase, adenosine nucleoside Let Ajay flow.

Among the enzymes that act on acid anhydrides are, for example, those that act on phosphorus- or sulfonyl-containing anhydrides. Some examples of enzymes that act on acid anhydrides are inorganic diphosphatases, trimetaphosphatase, adenosine-triphosphatase, apyrase, nucleoside-diphosphatase, acylphosphata Ases, nucleotide dephosphatase, endopolyphosphatase, exopolyphosphatase, nucleoside phosphoacylhydrolase, triphosphatase, CDP-diacylglycerol-diphosphatase, undecaprenyl Diphosphatase, dollykill diphosphatase, oligosaccharide-diphosphodolol diphosphatase, heterotrimatic G-protein GTPase, small monomeric GTPase, dinamin GTPase , Tubulin GTPase, diphosphoinositol-polyphosphate diphosphatase, H ⁺ -exporting ATPase, monosaccharide-transporting ATPase, maltose-exporting ATPase, glycerol-3-phosphate -Transporting ATPase, oligopeptide-transporting ATPase, polyamine-transporting ATPase, peptide-transporting ATPase, polyamine-transporting ATPase, peptide-transporting ATPase, fatty acid-acyl-CoA-transporting ATPases, protein-secreting ATPases, and the like.

The most preferred enzymes of the present invention are those which act on ester bonds, and include carboxylic acid ester hydrolases, thioester hydrolases, phosphate ester hydrolases, sulfate ester hydrolases and ribonucleases. Some examples of enzymes that act on ester bonds include acetyl-CoA hydrolase, palmitoyl-CoA hydrolase, succinyl-CoA hydrolase, 3-hydroxyisobutyryl-CoA hydrolase, Hydroxymethylglutaryl-CoA hydrolase, hydroxyacylglutathione hydrolase, glutathione thiol esterase, formyl-CoA hydrolase, acetoacetyl-CoA hydrolase, S -formylglutathione hydrolase, S Succinylglutathione hydrolase, oleyl- [acyl-carrier-protein] hydrolase, ubiquitin thiol esterase, [citrate- ( pro- 3S ) -lyase] thiol esterase, ( S ) -methylmalonyl-CoA hydrolase, ADP-dependent short-chain-acyl-CoA hydrolase, ADP-dependent heavy-chain-acyl-CoA hydrolase, acyl -CoA hydrolase, dodecanoyl- [acyl-carrier-protein] hydrolase, palmitoyl- (protein) hydrolase, 4-hydroxybenzoyl-CoA thioesterase, 2- (2-hydroxy-phenyl Benzenesulfinate hydrolase, alkaline phosphatase, acid phosphatase, phospho-serine phosphatase, phosphatidate phosphatase, 5'-nucleotidase, 3'-nucleotidase, 3 '(2'), 5'-biphosphate nucleotidase, 3-phytase, glucose-6-phosphatase, glycerol-2-phosphatase, phosphoglycerate phosphatase, Glycerol-1-phosphatase, mannitol-1-phosphatase, sugar-phosphatase, sucrose-phosphatase, inositol-l ( 4) Mono phosphatase, 4-phytase, phosphatidyl glycerophosphate with phosphatase, ADP phosphoglycerate phosphatase, N-acyl-9-New laminate phosphatase, nucleotidase kinase, polynucleotide 3 '-Phosphatase, [glycogen-synthase-D] phosphatase, [pyruvate dehydrogenase (lipo-amide)]-phosphatase, [acetyl-CoA carboxylase] -phosphatase, 3-deoxy-manno-to oktul bovine carbonate-8-phosphatase, polynucleotide 5'-phosphatase, sugar-terminal (sugar-terminal) - phosphatase, phosphatase as alkyl glyceryl acetyl, 2- Deoxyglucose-6-phosphatase, glycosylglycerol 3-phosphatase, 5-phytase, phosphodiesterase I, glycerophosphocholine phosphodiesterase, phospholipase C, phospholipase D, phosphoi Noctiated Phospholipase C, Sphingomyelin Po Podiesterase, glycerophosphocholine choline phosphodiesterase, alkylglycerophosphoethanolamine phosphodiesterase, glycerophosphinositol glycerophosphodiesterase, arylsulfatase, steryl-sulfatase, glycosulfata Azedes, choline-sulfatases, cellulose-polysulfatases, monomethyl-sulfatases, D-lactate-2-sulfatases, glucuronate-2-sulfatases, prenyl-diphosphatas Azede, aryldialkylphosphatase, diisopropyl-fluorophosphatase, oligonucleotidase, poly (A) -specific ribonuclease, yeast ribonuclease, deoxyribonuclease (pyrimidine dimer), Pisa Room poly three palrum (Physarum polycephalum) it is a ribonuclease, ribonuclease alpha, Aspergillus (Aspergillus) nuclease S, Serratia sense Marseille (Serratia marcescens) nuclease and the like.

The most preferred enzymes acting on the ester bonds are carboxyl esterase, aryl esterase, triacylglycerol lipase, phospholipase A ₂ , lyso-phospholipase, acetyl esterase, acetylcholinesterase, choline esterase, tropin esterase, pectin esterase , Sterol esterase, chlorophyllase, L-arabinonolactonase, gluconolactonase, uronolactonase, tanase, retinyl-palmitate esterase, hydroxybutyrate-dimer hydrolase, acylglycerol Lipase, 3-oxoadipate enol -lactonase, 1,4-lactonase, galactolipase, 4-pyridoxolactonase, acylcarnitine hydrolase, aminoacyl-tRNA hydrolase, D-arabi Nonomuria Lactobacillus better claim, 6-phospho-glucono-galactosidase better claim, phospholipase A _l, 6-acetyl-glucose Acetylase, lipoprotein lipase, dehydrocoumarin hydrolase, limonin-D-ring-lactonase, steroid-lactonase, triacetate-lactonase, actinomycin lactonase, orselinate- Deep seed hydrolase, cephalosporin-C deacetylase, chlorogenate hydrolase, α-amino acid esterase, 4-methyloxaloacetate esterase, carboxymethylene butenolidease, deoxyrimonate A-ring- Lactonase, 1-alkyl-2-acetylglycerophosphocholine esterase, fusarinine-C ornithine esterase, cinapine esterase, wax-ester hydrolase, phorbol-diester hydrolase, phosphatidylinositol dia Silases, sialate O -acetylesterases, acetoxybutynylbithiophene deacetylases, acetylsalicylate deacetylases, Methyllumbeliferyl-acetate diacetylase, 2-pyrone-4,6-dicarboxylate lactonase, N -acetylgalactoseaminoglycan deacetylase, juvenyl-hormone esterase, bis (2- ethylhexyl) phthalate esterase, protein-glutamate methyl esterase, 11-cis-retinyl-palmitate hydroxide roller dehydratase, all (all) - trans-retinyl-palmitate hydroxide roller dehydratase, -1 L- person Nonomuria (rhamnono) , 4-lactonase, 5- (3,4-diacetoxybut-1-ynyl) -2,2'-bithiophene deacetylase, fatty acid-acyl-ethyl-ester synthase, xylono ) -1,4-lactonase, setlaxate benzyl esterase, acetylalkylglycerol acetylhydrolase, acetylxsilane esterase, feruloyl esterase, cutinase, poly (3-hydroxybutyrate) dipolymerase , Poly (3-hydroxyoctanoate) dipolymerase, ah A hydroxy carboxylic ester roller azepin acids such as aldehyde esterase-oxy-acyl hydroxy roller dehydratase, poly New naphthyridine.

Thus, enzymes that act on ether bonds include trialkylsulfonium hydrolases and ether hydrolases. Enzymes that act on ether bonds can act on both thioether bonds and oxygen equivalents. Specific enzyme examples belonging to these groups include adenosyl homocysteinase, adenosylmethionine hydrolase, isochorismatase, alkenylglycerophosphocholine hydrolase, epoxide hydrolase, trans -epoxysuccinate Hydrolase, alkenylglycerophosphoethanolamine hydrolase, leukotriene-A ₄ hydrolase, hepoxylin-epoxide hydrolase and limonene-1,2-epoxide hydrolase.

Among the enzymes that act on the carbon-nitrogen bonds are linear amides, cyclic amides, linear amidines, cyclic amidines, nitriles and other compounds. Specific examples in these groups include asparaginase, glutaminase, ω-amidase, amidase, urease, β-ureidopropionase, arylformamidase, biotinidase, aryl- Acylamidase, amino-acylase, aspartoacylase, acetylornithine deacetylase, acyl-lysine diacylase, succinyl-diaminopimelate desuccinase, pantothenase, ceramida Azease, Coloylglycine Hydrolase, N-acetylglucosamine-6-phosphate deacetylase, N -acetylmuramoyl-L-alanine amidase, 2- (acetamidomethylene) succinate hydrolase, 5 -Aminopentanamidase, formylmethionine deformylase, hypohydrate hydrolase, N -acetylglucosamine deacetylase, D-glutaminase, N -methyl-2-oxoglutamate hydrolase, Glutamine -(Asparagine) ase, alkylamidase, acylagmatin amidase, chitin deacetylase, peptidyl-glutaminase, N -carbamoyl-sarcosine amidase, N (long-chain- Acyl) ethanolamine diasilase, mimosinase, acetyl-putrescine deacetylase, 4-acetamidobutyrate deacetylase, theanine hydrolase, 2- (hydroxymethyl) -3- (acetyl) Amidomethylene) succinate hydrolase, 4-methyleneglutaminase, N -formylglutamate diformillase, glycosphingolipid diasilase, aquilacin-A diacylase, peptide diformilla Azede, dihydropyrimidinase, dehydrourotase, carboxymethyl-hydantoinase, creatininase, L-lysine-lactamase, arginase, guanidinoacetase, creatinase , Allantoicase, cytosine deaminase, li A propane-1-carboxylate deaminase - Plastic rain dehydratase, thiazol Mina kinase, l- aminocyclohexane.

Some preferred enzymes of the invention belong to the group of enzymes that act on peptide bonds, which group is also referred to as peptidase. Peptidases can be further separated into exopeptidases that act only near the terminal end of the polypeptide chain and endopeptidases that act internally within the polypeptide chains. Enzymes that act on peptide bonds are aminopeptidases, dipeptidases, di- or tri-peptidyl-peptidases, peptidyl-dipeptidases, serine-type carboxypeptidases, metallocarboxypeptidases, cysteine-types Enzymes selected from the group of carboxypeptidases, omega peptidases, serine endopeptidases, cysteine endopeptidases, aspartic endopeptidases, metalloendopeptidases, and threonine endopeptidases. Some specific examples of enzymes belonging to these groups include cystinyl aminopeptidase, tripeptide aminopeptidase, prolyl aminopeptidase, arginyl aminopeptidase, glutamyl aminopeptidase, cytosol alanyl aminopeptidase, lysyl aminopeptidase, Met-X Dipeptidase, Non-stereospecific Dipeptidase, Cytosol Nonspecific Dipeptidase, Membrane Dipeptidase, Dipeptidase E, Dipeptidyl-peptidase I, Dipeptidyl-peptidase, Tripeptidyl-peptidase I, Tripeptidyl-peptidase II , X-Pro dipeptidyl-peptidase, peptidyl-dipeptidase A, lysosomal Pro-X carboxypeptidase, carboxypeptidase C, acylaminoacyl-peptidase, peptidyl-glycine amidase, β-aspartyl-peptidase, ubiquit Quintinyl Hydrolase 1, Chymotrypsin, Chymotrypsin C, Metridine, Trypsin, Throm , Plasmin, enteropeptidase, acrosine, α-lytic endopeptidase, glutamyl endopeptidase, cathepsin G, curcumycin, prolyl oligopeptidase, brachyurin, plasma kallikrein, tissue kallikrein, Pancreatic elastase, leukocyte elastase, chymase, cerevisin, hippodermin C, lysyl endopeptidase, endopeptidase La, γ-renin, venombin AB, leucine endopeptidase, trypsin Tasase, squaterin, leucine, subtilisin, origin, endopeptidase K, thermomicholine, thermitase, endopeptidase So, t-plasminogen activator, protein C (activated), Pancreatic endopeptidase E, pancreatic elastase II, IgA-specific serine endopeptidase, u-plasminogen activator, venombin A, furin, myeloblastin, semenogellase, granzyme ) A, that Lanzyme B, Streptogrisine A, Streptogrisine B, Glutamyl Endopeptidase II, Oligopeptidase B, Omphtin, Togavirine, Flavivirin, Endopeptidase Clp, Proprotein Convertase 1, Protein convertase 2, lactosepin, assembler, hepacivirin, spheromosin, pseudomonasin, santomonasin, C-terminally treated peptidase, physarolisin, cathepsin B, papain, Picaine, chymopapine, asclepine, clostripine, streptopine, actinidine, cathepsin L, cathepsin H, cathepsin T, glycine endopeptidase, tumor procoagulant, cathepsin S, picorine 3C, picorin 2A, caricine, ananaine, stem bromelain, fruit bromelain, legumain, histolysine, caspase-1, gingifain R, cathepsin K, adenine, bleomycin Hydrolase, cathepsin F, cathepsin O, cathepsin V, -Inclusion-α-endopeptidase, helper-component proteinase, L-peptidase, gingipine K, staphopine, separase, V-cath endopeptidase, croupifa Phosphorus, calpine-1, calpine-2, pepsin A, pepsin B, gastricin, chymosin, cathepsin D, nepenthesin, renin, pro-opiomelanocortin converting enzyme, aspergillopepcine I, Aspergillopepsin II, Penicillopepsin, Rizopuspepsin, Endopsipsin, Mucopepsin, Candida-Pepsin, Saccharopepsin, Rhodorulapepsin, Acrosilopepsin, Polyporopepsin, Pycnopelopepsin, SKI Thalidopepsin A, Schitalipopepsin B, Cathepsin E, Barrier Pepsin, Signal Peptidase II, Plaspecin I, Plascinsin II, Pipthecin, Yapsin 1, Termoxin, Prephylline Peptidase, Nodavirus Endo Peptidase, memacin 1, memacin 2, atolicin A, microbial collagenase, Coricin (leucolysin), stromericin 1, meprine A, procollagen C-endopeptidase, astaxin, pseudolysine, thermolysin, basilillin, aureolysin, cocoicin, mycolysine, gel Latina B, Leishmanolysin, Saccharin, Gamethorin, Cetaricin, Horicin, Ruberlycin, Botropasin, Oligopeptidase A, Endothelin-Converting Enzyme, AD-AM10 Endopeptidase Enzymes selected from the group of et al.

Suitable enzymes that act on carbon-carbon bonds, which can be found in ketonic substances, are oxaloacetase, fumarylacetoacetase, kynureninase, floretine hydrolase, acylpyru Bait hydrolase, acetylpyruvate hydrolase, β-diketone hydrolase, 2,6-dioxo-6-phenylhexa-3-enonate hydrolase, 2-hydroxymuconate-semialdehyde hydroxide Rollases and cyclohexane-1,3-dione hydrolases, including but not limited to.

Examples of enzymes in the group that act on halide bonds include alkylhalidase, 2-haloacid dihalogenase, haloacetate dihalogenase, thyroxine diiodinase, haloalkanes dihalogenase, 4-chlorobenzoate dihalogenase, 4-chlorobenzoyl-CoA dihalogenase, atrazine chlorohydrolase and the like.

Further examples according to the invention of enzymes which act on specific bonds are phosphoamidase, N -sulfoglucosamine sulfohydrolase, cyclamate sulfohydrolase, phosphonoacetaldehyde hydrolase, phosphonoacetate hydrolase Azedes, trithionate hydrolases, UDP sulfoquinobose synthase and the like.

According to the present invention, the enzymes added to the biodegradable chewing gum may be one kind or different kinds combined.

Some enzymes require co-factors to take effect. Examples of such co-factors are 5,10-methenyltetrahydrofolate, ammonia, ascorbate, ATP, bicarbonate, bile salts, biotin, bis (molybdoterin guanine dinucleotide) molybdate Denium cofactor, cadmium, calcium, cobalamin, cobalt, coenzyme F430, coenzyme-A, copper, dipyromethane, dithiothreitol, divalent cation, FAD, flavin, flavoprotein, FMN, glutathione, heme ), Heme-thiolate, iron, iron (2+), iron-molybdenum, iron-sulfur, lipoyl group, magnesium, manganese, metal ions, molybdenum, molybdopterin, monovalent cation, NAD, NAD (P) H, Nickel, Potassium, PQQ, Protohem IX, Pyridoxal-Phosphate, Pyruvate, Selenium, Sirohem, Sodium Tetrahydropteridine, Thiamine Diphosphate, Topaquinone, Tryptophan Tryptophilquinone (TTQ) , Tungsten, vanadium and zinc.

In accordance with general principles in the preparation of the embodiments which fall within the scope of the invention, variations of the suitable components are listed and described below.

Chewing gums according to the present invention may comprise coloring agents. According to an embodiment of the present invention, the chewing gum may comprise colorants and whiteners such as FD & C-type dyes and lakes, fruit and vegetable extracts, titanium dioxide and combinations thereof. have. Other useful chewing gum base components include antioxidants such as butylated hydroxytoluene (BHT), butyl hydroxyanisole (BHA), propyl gallate and tocopherols, and preservatives.

In an embodiment of the invention, the chewing gum comprises softeners in an amount of about 0 to about 18% by weight of the chewing gum, more typically in an amount of about 0 to about 12% by weight of the chewing gum.

According to the present invention, emollients / emulsifiers may be added to the chewing gum and gum base.

According to the present invention, gum base formulations comprise one or more softeners, for example sucrose polyesters, tallow, disclosed in WO 00/25598, incorporated herein by reference. Hydrogenated tallo, hydrogenated vegetable oils and partially hydrogenated vegetable oils, cocoa butter, degreased cocoa powder, glycerol monostearate, glycerol triacetate, lecithin, mono-, di- and triglycerides, acetylated Monoglycerides, fatty acids (eg, stearic acid, palmitic acid, oleic acid and linoleic acid) and combinations thereof. As used herein, the term "softner" refers to a component that softens gum base or chewing gum formulations and refers to waxes, fats, oils, emulsifiers, surfactants and solulizers. Include.

In order to soften the gum base, give the gum base a good smooth surface and provide moisture-binding properties that reduce the adhesive properties, one or more emulsifiers are typically 0-18% of the weight of the gum base, preferably gum It is added to the composition in an amount of 0-12% of the weight of the base. Mono- and diglycerides of edible fatty acids, lactic acid esters and acetic acid esters of mono- and diglycerides of edible fatty acids, acetylated modo and di-glycerides, sugar esters of edible fatty acids, Na- , K-, Mg- and Ca-stearates, lecithin, hydroxide lecithin and their equivalents are examples of commonly used emulsifiers that can be added to the chewing gum base. If a biological or pharmaceutically active ingredient as defined below is present, the formulation may comprise certain emulsifiers and / or solubilizers to disperse and release the active ingredient.

In preparing chewing gum bases, waxes and fats are commonly used for adjustment of consistency and softening of chewing gums. In connection with the present invention, any commonly used suitable types of waxes and fats such as rice bran wax, polyethylene wax, petroleum wax (purified paraffin and microcrystalline wax), paraffin, beeswax, carnauba Any suitable oil or fat may be used, such as waxes, candelilla waxes, cocoa butter, skimmed cocoa powder and for example fully or partially hydrogenated vegetable oils or fully or partially hydrogenated animal fats.

In an embodiment of the invention, the chewing gum comprises a filler.

If desired, chewing gum base formulations include, for example, silicate compounds such as magnesium and calcium carbonate, sodium sulfate, ground limestone, magnesium and aluminum silicate, kaolin and clay, aluminum oxide, silicon oxide, One or more fillers / texturizers including talc, titanium oxide, mono-, di-, and tri-calcium phosphates, cellulose polymers such as wood, and combinations thereof.

In an embodiment of the invention, the chewing gum comprises filler in an amount of about 0 to about 50% of the weight of the chewing gum, more typically in an amount of about 10 to about 40% of the weight of the chewing gum.

In the present invention, chewing gum components are for example bulk sweeteners, high-concentration sweeteners, flavoring agents, emollients, emulsifiers, colorants, binders, acidulants, fillers, antioxidants and It may contain other ingredients such as pharmaceutically or biologically active substances that impart the desired properties to the finished chewing gum product.

Suitable bulk sweeteners include sugar and sugarless sweetening compounds. Bulk sweeteners typically comprise an amount of about 5 to about 95% of the weight of the chewing gum, more typically an amount of about 20 to about 80%, such as 30 to 60% of the weight of the gum.

Useful sugar sweetners include sucrose, dextrose, maltose, dextrins, trehalose, D-tagatose, dried invert sugar, used alone or in combination, Saccharide-containing compounds generally known in the chewing gum art, including, but not limited to, fructose, rebulose, galactose, corn syrup solids, and the like.

Sorbitol can be used as an unsweetened sweetener. Other useful sugarless sweeteners include, but are not limited to, other sugar alcohols such as mannitol, xylitol, hydrogenated starch hydrolysates, maltitol, isomalthol, erythritol, lactitol and the like, used alone or in combination.

High-intensity artificial sweetening agents may also be used alone or in combination with the sweeteners. Preferred high-concentration sweeteners are sucralose, aspartame, salts of acefulpam, alitams, saccharin and salts thereof, cyclamic acid and salts thereof, glycyrrhizin, dihydrochalcones, taumate, used alone or in combination , Monoline, sterioside, and the like. In order to provide longer lasting sweetness and flavor recognition, it may be useful to encapsulate or control the release of at least a portion of the artificial sweetener. Granulation, wax granulation, spray drying, spray chilling, fluid bed coating, coascervation, encapsulation in yeast cells and fiber extrusion Techniques such as can be used to achieve the desired emission characteristics. Encapsulation of sweeteners may also be provided using another chewing gum component, such as a resinous compound.

The amount of artificial sweetener can vary considerably and will depend on factors such as the efficacy of the sweetener, the rate of release, the desired sweetness of the product, the level and type and cost of the flavor used. Thus, the activity level of artificial sweetener may vary from about 0.02 to about 30% by weight, preferably from 0.02 to about 8% by weight. If carriers used for encapsulation are included, the dose level of encapsulated sweetener will be proportionally higher. Combinations of sugar and / or sugar free sweeteners can be used in chewing gum formulations treated in accordance with the present invention. In addition, emollients such as sugar or alditol solutions also provide additional sweetness.

If a low calorie gum is desired, a low calorie bulking agent can be used. Examples of low-dose bulking agents include polydextrose, Raftilose, Raftilin, Fructooligosaccharides (NutraFlora ^® ), Palatinos oligosaccharides; Guar gum hydrolysates (eg Sun Fiber ^® ) or indigestible dextrins (eg Fiber ^® ). However, other low-dose bulking agents can be used.

Chewing gums according to the present invention include natural and synthetic flavorings in the form of natural vegetable ingredients, essential oils, essences, extracts, powders, including, for example, acids and other substances that may affect the aesthetic profile. It may include fragrances and flavoring agents. Examples of liquid and powdered flavors include coconut, coffee, chocolate, vanilla, grapefruit, orange, lime, menthol, liquorice, caramel aroma, honey aroma, peanuts, walnuts, cashews, hazelnuts, Essences from almonds, pineapples, strawberries, raspberries, tropical fruits, cherries, cinnamon, peppermint, wintergreen, spearmint, eucalyptus, and mints, apples, pears, peaches, strawberries, apricots, raspberries, cherries, pineapples And fruit essences such as plum essences. Essential oils include peppermint, spearmint, menthol, eucalyptus, clove oil, bay oil, anise, thyme, cedar leaf oil, nutmeg, and oils of the aforementioned fruits. Include.

The chewing gum flavor may be a natural flavor, lyophilized and preferably in the form of powder, slices, or pieces or combinations thereof. The particle size calculated as the longest size of the particles may be less than 3 mm, less than 2 mm, or more preferably less than 1 mm. Natural flavors may be in the form of 3 μm to 2 mm, with particle sizes such as 4 μm to 1 mm. Preferred natural flavorings include seeds of fruits such as strawberries, blackberries and raspberries.

Various synthetic flavors, such as mixed fruit flavors, can be used in the chewing gum core of the present invention. As mentioned above, the fragrance may be used in smaller amounts than those conventionally used. Perfumes and / or flavors may be used in amounts of from 0.01 to about 30% of the weight of the final product, depending on the desired strength of the perfume and / or flavor used. Preferably the content of fragrance / flavour is in the range of 0.2 to 3% of the weight of the total composition.

In an embodiment of the present invention, flavoring agents include natural and synthetic flavorings in the form of natural vegetable ingredients, essential oils, essences, extracts, powders, including acids and other substances that may affect aesthetic profile. It may include fragrances and flavoring agents.

Other chewing gum ingredients, which may be included in the chewing gum according to the invention, are surfactants and / or solubilizers, especially when pharmaceutically or biologically active ingredients are present. For examples of the types of surfactants to be used as solubilizers in the chewing gum compositions according to the invention, see H.P. See Fiedler, Lexikon der Hilfstoffe fur Pharmacies, Kosmetik und Angrenzende Gebiete, pages 63-64 (1981), and a list of approved food emulsifiers in individual countries. Anionic, cationic, amphoteric or nonionic solubilizers can be used. Suitable solubilizers include lecithin, polyoxyethylene stearate, polyoxyethylene sorbitan fatty acid esters, fatty acid salts, mono and diglycerides of edible fatty acids, diacetyl tartaric acid esters of edible fatty acids, mono and diglycerides of edible fatty acids. Citric acid esters, saccharose esters of fatty acids, polyglycerol esters of fatty acids, polyglycerol esters of interesterified castor oil (E476), sodium stearoylate, sodium lauryl sulfate and fatty acids Sorbitan esters and polyoxyethylated and hydrogenated castor oil (e.g., products sold under the trade name CREMOPHOR), block copolymers of ethylene oxide and propylene oxide (e.g., PLURONIC and POLOXAMER Products sold under the trade name), polyoxyethylene fatty acid alcohol Teres, polyoxyethylene sorbitan fatty acid esters, sorbitan esters of fatty acids, and polyoxyethylene stearic acid esters.

Particularly useful solubilizers are, for example, polyoxyethylene stearates such as polyoxyethylene (8) stearate and polyoxyethylene (40) stearate, for example TWEEN 20 (monolaurate). Polyoxyethylene sorbitan fatty acid esters sold under the trade name Tween, such as Tween 80 (Monooleate), Tween 40 (Monopalmitate), Tween 60 (Monostearate) or Tween 65 (Tristearate) , Mono and diacetyl tartaric acid esters of edible fatty acids, mono and diacetyl tartaric acid esters, citric acid esters of mono and diglycerides of edible fatty acids, sodium stearoylate, sodium lauryl sulfate, polyoxyethylation Block copolymers of hydrogenated castor oil, ethylene oxide and propylene oxide and polyoxyethylene fatty acid alcohols A hotel. The solubilizer may be a single compound or a combination of several compounds. In the presence of the active ingredient, the chewing gum preferably also comprises a carrier known in the art to which this invention belongs.

12H₂0) 및 붕소, 바륨, 스트론튬, 철, 칼슘, 아연(아세트산 아연, 염화 아연, 글루콘산 아연), 구리(염화 구리, 황산 구리), 납, 은, 마그네슘, 나트륨, 칼륨, 리튬, 몰리브덴, 바나듐과 같은, 제한된 수용해도를 갖는 금속 염류, 복합체류 및 화합물들; 구강 및 치아의 관리를 위한 기타 조성물들: 예를 들면, 불소(예를 들면, 불화 나트륨, 소디움 모노플루오로포스페이트, 아미노플루오리드류, 불화 제1주석), 인산염류, 탄산염류 및 셀렌을 포함하는 염류, 복합체류 및 화합물들. 다른 활성 물질들은 J. Dent. Res. Vol. 28 No. 2, pages 160-171, 1949에서 찾을 수 있다.In one embodiment, the chewing gum according to the present invention comprises a pharmaceutically, cosmetically or biologically active material. Examples of such active substances, examples of substances found in WO OO / 25598, hereby incorporated by reference, include drugs, dietary supplements, preservatives, pH-controlling agents, non-smoking agents. And substances capable of releasing urea during chewing and substances for the care or treatment of the oral cavity and teeth, such as hydrogen peroxide. Examples of useful active substances in the form of preservatives include salts and derivatives of guanidine and biguanide (eg chlorhexidine diacetate) and materials of the following types with limited water solubility: quaternary ammonium compounds (E.g., ceramine, chloroxylinol, crystal violet, chloramine), aldehydes (e.g. paraformaldehyde), derivatives of dequaline, polyoxylin, phenols (e.g. , Thymol, p-chlorophenol, cresol), hexachlorophene, salicylic anilide compounds, triclosan, halogens (iodine, iodophores, chloramines, dichlorocyanuric salts) acid salts)), alcohols (3,4 dichlorobenzyl alcohol, benzyl alcohol, phenoxyethanol, phenylethanol), (see Martindale, The Extra Pharmacopoeia, 28th edition, pages 547-578); Aluminum salts (for example aluminum potassium sulfate AlK (SO ₄ ) ₂

12H ₂ 0) and boron, barium, strontium, iron, calcium, zinc (zinc acetate, zinc chloride, zinc gluconate), copper (copper chloride, copper sulfate), lead, silver, magnesium, sodium, potassium, lithium, molybdenum Metal salts, complexes and compounds having limited water solubility, such as vanadium; Other compositions for the care of the oral cavity and teeth include, for example, fluorine (eg sodium fluoride, sodium monofluorophosphate, aminofluorides, stannous fluoride), phosphates, carbonates and selenium Salts, complexes and compounds. Other active substances are described in J. Dent. Res. Vol. 28 No. 2, pages 160-171, 1949.

Examples of active substances in the form of pH-controlling agents in the oral cavity are acids such as adipic acid, succinic acid, fumaric acid or salts thereof, or salts of citric acid, tartaric acid, malic acid, acetic acid, lactic acid, phosphoric acid and glutaric acid and carboxylic acid Acceptable bases such as carbonates, hydrogen carbonates, phosphates, sulfates or oxides of sodium, potassium, ammonium, magnesium, or calcium, especially oxides of magnesium and calcium.

Active ingredients include, but are not limited to, the compounds described below or derivatives thereof: acetaminophen, acetylsallicylsyre, buprenorphine bromhesin Buphenorphine Bromhexin Celcoxib Codeine, diphene Diphenhydramin, Diclofenac, Etoricoxib, Ibuprofen, Ibuprofen, Indometacin, Ketoprofen, Lumiracoxib, Morphine, Naproxen, Oxycodon, Parecoxib, Piroxicam, Pseudoefedrin, Rofecoxib, Tenoxicam, Tramadol, Tramadol Valdecoxib, Calciumcarbonate, Magaldrate, Disulfiram, Bupropion, Nicotine, Azithromycin, Clarithromycin , Clotrimazole, Erythromycin, Tetracycline, Granisetron, Ondansetron, Prometazin, Tropisetron, Bromphenamine (Brompheniramine), ceterizin (Ceterizin), leco-Ceterizin, Chlorcyclizine, Chlorpheniramin, Difenhydramine, Doxylamine, Phenofemin Fenofenadin, Guaifenesin, Loratidin, Des-Loratidin, Phenyltoloxamine, Promethazin, Pyridamine, Terpenadine Terfenadin, Troxerutin, Methyldopa, Methylphenidate, Benzalcon Chloride, Benzat Chloride. Chloride, Cetylpyrid.Chloride, Chlorhexidine, Ecabet-sodium, Haloperidol, Allopurinol, Colchinine, Theophylline ), Propanolol, Prednisolone, Prednisone, Fluoride, Urea, Miconazole, Actot, Gibenclamide, Article Lipizide, Metformin, Miglitol, Miglitol, Repaglinide, Rosiglitazone, Apomorfin, Cialis, Sildenafil, Sildenafil, Vardenafil ), Diphenoxylate, Simethicone, Cimetidine, Camotidine, Famotidine, Ranitidine, Latinindine, Ratinidine, cetrizin, Loratadine , Aspirin, Benzocaine, Dextrose Dextrometorphan, Ephedrine, Phenylpropanolamine, Pseudoephedrine, Cisapride, Domperidone, Metoclopramide, Acyclovir, Acyclovir Dioctylsulfosuccinate (Dioctylsulfosucc.), Phenolphtalein, Almotriptan, Eletriptan, Ergotamine, Migea, Nagetriptan, Lizatriptan Tan, sumatriptan, zolmitriptan, aluminum salts, calcium salts, iron salts, silver salts, zinc-salts, amphotericin B, chlorhexidine, myconazole, triamcinolone acetonide, melatonin, phenobarbitol, caffeine, benzodiazepiner , Hydroxyzine, meprobamate, phenothiazine, buclizine, bromethazine, cinnarizine, cyclizine, diphenhydramine, dimenhydramine, buflomedil, amphetamine, caffeine, ephedrine, Erystatt, phenylephedrine, phenylpropanolamine, pseudoephedrine, sibutramine, ketoconazole, nitroglycerin, nystatin, progesterone, testosterone, vitamin B12, vitamin C, vitamin A, vitamin D, vitamin E, pilocarpine, aluminum amino acetate, cimetidine , Esomeprazole, pamotidine, lansoprazole, magnesium oxide, nizamide and / or latininidine.

In general, the chewing gum and gum bases prepared according to the present invention are preferably based only on biodegradable polymers. However, within the scope of the present invention, other conventional chewing gum elastomers or elastomeric plasticizers may be applied. Thus, in embodiments of the invention, the at least one biodegradable polymer comprises at least 5% and at least 90% of the chewing gum polymers and the remaining polymers are natural resins, synthetic resins and / or synthetic elastomers, such as Polymers generally considered non-biodegradable.

In an embodiment of the invention, the natural resin is a terpene resin, for example terpene resins derived from alpha-pinene, beta-pinene, and / or d-limonene, natural terpene resins, gum rosin, tall oil rosin (tall oil rosins), glycerol esters of wood rosin or partially hydrogenated rosin, glycerol esters of polymerized rosin, glycerol esters of partially dimerized rosin, pentaerythritol esters of partially hydrogenated rosin Other derivatives such as methyl esters of rosin, partially hydrogenated methyl esters of rosin, or pentaerythritol esters of rosin, and combinations thereof.

In an embodiment of the invention, the synthetic resin comprises polyvinyl acetate, vinyl acetate-vinyl laurate copolymers and mixtures thereof.

Generally within the scope of the present invention, useful synthetic elastomers include synthetic elastomers listed in US Food and Drug Administration (FDA) CFR, Title 21, Section 172,615, the Masticatory Substances, Synthetic, for example, in the range of 50,000 to 80,000. Polyisobutylene, isobutylene-isoprene copolymer (butyl elastomer), styrene-butadiene copolymers having a gas pressure chromatography (GPC) average molecular weight in the range of about 10,000 to 1,000,000, including, for example, about 1: 3 Copolymers having styrene-butadiene ratios of from 3: 1, polyvinyl acetate (PVA), for example polyvinyl having a GPC average molecular weight in the range of 2,000 to 90,000, such as 3,000 to 80,000, including the range of 30,000 to 50,000 Acetate, polyisoprene, polyethylene, when higher molecular weight polyvinyl acetates are commonly used in balloon gum base Vinyl acetate-butyl laurate copolymers such as, but not limited to, copolymers having a vinyl laurate content of about 5 to 50%, such as 10 to 45% of the weight of the copolymer and combinations thereof.

It is conventional in the art to combine low molecular weight elastomers with synthetic elastomers having high molecular weight at the gum base. Currently preferred combinations of synthetic elastomers include polyisobutylene and styrene-butadiene, polyisobutylene and polyisoprene, polyisobutylene and isobutylene-isoprene copolymer (butyl rubber) and polyisobutylene, styrene-butadiene Combinations of copolymers and isobutylene isoprene copolymers and the individual synthetic polymers described above and mixtures thereof, respectively, mixed with polyvinyl acetate, vinyl acetate-vinyl laurate copolymers, but not limited thereto.

According to the present invention, as used herein, chewing gum base components may include one or more resinous compounds that contribute to the desired chewing properties and act as plasticizers for the elastomers of the gum base composition. In the present invention, useful elastomeric plasticizers include glycerol esters of partially hydrogenated rosin, glycerol esters of polymerized rosin, glycerol esters of partially dimerized rosin, glycerol esters of tall oil rosin, partially hydrogenated Natural rosin esters, often referred to as ester gums, including pentaerythritol esters of rosin, methyl esters of rosin, partially hydrogenated methyl esters of rosin, and pentaerythritol esters of rosin It doesn't work. Other useful resinous compounds include synthetic resins such as alpha-pinene, beta-pinene, and / or d-limonene, terpene resins derived from natural terpene resins; And suitable combinations of the foregoing. The choice of elastomeric plasticizers can vary depending on the specific application and the type of elastomer used.

An external coating may be provided on the chewing gum according to the invention. Applicable hard coatings may be selected from the group consisting of sugar coatings and sugarless coatings and combinations thereof. The hard coating may comprise, for example, 50 to 100% by weight of a polyol selected from the group consisting of sorbitol, maltitol, mannitol, xylitol, erythritol, lactitol and isomalt and variants thereof. have. In an embodiment of the invention, the outer coating is an edible film comprising one or more components selected from the group consisting of edible film-forming agents and waxes. Film formers can be selected from the group consisting of, for example, cellulose derivatives, modified starches, dextrins, gelatin, shellac, gum arabic, zein, vegetable gums, synthetic polymers, and combinations thereof. In an embodiment of the invention, the outer coating may comprise a binder, a water-absorbing component, a film-forming agent, a dispersing agent, an antisticking component, a bulking agent, a flavoring agent, a colorant, a pharmaceutically or cosmetically active ingredient, At least one additive component selected from the group consisting of agents capable of catalyzing post-chewing degradation of lipid components, wax components, sugars, acids and degradable components.

In another embodiment of the invention, the outer coating is a soft coating. Soft coatings may include sugar free coating agents.

Unless otherwise indicated, as used herein for polymers, the term "molecular weight" means a numerical average molecular weight (Mn) in g / mol. The acronym PD stands for polydispersity. Likewise, the molecular weight of the enzyme is given in kilodaltons expressed in kDa.

The glass transition temperature (Tg) can be determined, for example, by differential scanning calorimetry (DSC). DSC is generally applied to determine and study thermal transitions of polymers, specifically this technique involves secondary transitions of materials, ie changes in heat capacity, but latent heat ) Can be applied for the determination of thermal transitions without. The glass transition is a second-order transition.

The invention is described with reference to the following figures showing the formation of decomposition products measured by head space GC / MS:

1 shows the formation of compounds a and b in chewing gum comprising glucose oxidase.

2 depicts the formation of compounds a and b in chewing gum comprising neutrases.

3 shows the formation of compounds a and b in chewing gum comprising bromelain.

4 shows the formation of compounds a and b in chewing gum comprising trypsin.

The following non-limiting examples illustrate the preparation of chewing gum according to the present invention.

Example  One

Ring open To polymerization  due to Obtained  Preparation of Polyester Elastomers

Elastomer samples were synthesized in a dried N ₂ glove box as follows. In a 500 mL resin kettle equipped with an overhead mechanical stirrer, a solution of 3.143 g pentaerythritol and 0.5752 g Sn (Oct) ₂ (1.442 g Sn (Oct) ₂ ) dissolved in 5 mL methylene chloride 2.0 ml) was charged under a dry N ₂ purge. Methylene chloride was evaporated under N ₂ purge for 15 minutes. Then, ε-caprolactone (1144 g, 10 mol), trimethylene carbide (31 g, 0.30 mol) and δ-valerolactone (509 g, 5.1 mol) were added. The resin kettle was immersed in a 130 ° C. oil bath and stirred for 13.9 hours. Thereafter, the kettle was taken out of the oil bath and cooled at room temperature. The solid elastic product was removed into small pieces using a knife and placed in a plastic container.

The properties of the product were M _n = 56,000 g / mol and M _w = 98,700 g / mol (gel permeation chromatography with on-line MALLS detector) and Tg = -58.9 ° C. (DSC, heating rate 10 ° C./min).

Example  2

Ring open To polymerization  due to Obtained  Preparation of Polyester Elastomers

Elastomer samples were synthesized in a dried N ₂ glove box as follows. In a 500 mL resin kettle equipped with an overhead mechanical stirrer, dried 3.152 g pentaerythritol and 0.5768 g Sn (Oct) ₂ (2.0 ml solution of 1.442 g Sn (Oct) ₂ dissolved in 5 mL methylene chloride) Was charged under an N ₂ purge. Methylene chloride was evaporated under N ₂ purge for 15 minutes. Then, ε-caprolactone (1148 g, 10 mol), trimethylene carbide (31 g, 0.30 mol) and δ-valerolactone (511 g, 5.1 mol) were added. The resin kettle was immersed in a 130 ° C. constant temperature oil bath and stirred for 13.4 hours. Thereafter, the kettle was taken out of the oil bath and cooled at room temperature. The solid elastic product was removed into small pieces using a knife and placed in a plastic container.

The properties of the product were M _n = 88,800 g / mol and M _w = 297,000 g / mol (gel permeation chromatography with on-line MALLS detector) and Tg = -59.4 ° C. (DSC, heating rate 10 ° C./min).

Example  3

Ring open To polymerization  due to Obtained  Preparation of Polyester Elastomers

Resin samples were prepared using a cylindrical glass 10L pilot reactor with a glass stirring shaft and a Teflon stirring blade and a bottom outlet and jacket. Heating of the reactor contents was carried out through a circulation of silicone oil, which was maintained at 130 ° C. through an outer jacket. ε- caprolactone (358.87g, 3.145 mol) and 1,2-propylene glycol (79.87g, 1.050 mol) of stannous loam acid as a catalyst ^- was charged to the reactor with (1.79g, 4.42 x10 ³ mole) of 130 The reaction was carried out at about 30 minutes. Thereafter, molten D, L-lactide (4.877 kg, 33.84 moles) was added and the reaction continued for about 2 hours. After completion of this reaction time, the base outlet was opened to allow the molten polymer to exit into a Teflon-lined paint can.

The properties of the product were M _n = 6,000 g / mol and M _w = 7,000 g / mol (gel permeation chromatography with on-line MALLS detector) and Tg = 25-30 ° C. (DSC, heating rate 10 ° C./min).

Example  4

Condensation  By step-growth polymerization Obtained  Preparation of Polyester Elastomers

Elastomer samples were prepared using a 500 mL resin kettle equipped with an overhead stirrer, nitrogen gas inlet tube, thermometer and distillation head for methanol removal. The kettle was charged with 83.50 g (0.43 mole) dimethyl terephthalate, 99.29 g (0.57 mole) dimethyl adipate, 106.60 g (1.005 mole) di (ethylene glycol) and 0.6 g calcium acetate monohydrate. Under nitrogen, the mixture was slowly heated with stirring until all the components melted (120-140 ° C.). Heating and stirring were continued and methanol was distilled off continuously. The temperature was slowly increased in the range of 150-200 ° C. until the evolution of methanol stopped. The heating was stopped and the contents cooled to about 100 ° C. The reactor lid was removed and the molten polymer was carefully poured into a receiving vessel.

The properties of the product were M _n = 40,000 g / mol and M _w = 190,000 g / mol (gel permeation chromatography with on-line MALLS detector) and Tg = -30 ° C. (DSC, heating rate 10 ° C./min).

Example  5

Preparation of gum base

The procedure for preparing the gum bases was carried out as follows: Elastomer and resin were added to the mixing kettle with mixing means such as horizontally arranged Z-shaped arms. The kettle was preheated to a temperature of about 60-80 ° C. for 15 minutes. The mixture was mixed for 10-20 minutes until the whole mixture was uniform. The mixture was then drained to a pan and cooled to room temperature from a discharge temperature of 60-80 ° C.

Two different gum bases were prepared as indicated in Table 1.

Sword base No. Suzy Elastomer 1 Elastomer 2 Ratio of Resin / Elastomer 1 / Elastomer 2 101 Resin Polymer of Example 3 Elastomer Polymer of Example 1 Elastomer Polymer of Example 2 55/30/15 102 Resin Polymer of Example 3 Elastomer Polymer of Example 4 - 60/40

Table 1: Gum Base Preparation.

Example  6

Chewing  Manufacture of sword

The gum bases of Example 5 were used in the preparation of the chewing gum with the basic formulations shown in Table 2. The formulations were identical except that the addition of enzyme was replaced by the same amount of sorbitol.

Table 2: Chewing Gum Formulations with Different Enzyme Concentrations. Peppermint flavor.

Component concentrations are given in weight percent.

Enzyme concentrations of 0.32, 0.8, 1.6, 4.8 and 14.4 weight percent of the total chewing gum formulation correspond to 1.0, 2.5, 5.0, 15.0 and 45.0 percent, respectively, for the gum base, which accounts for 32 weight percent of the chewing gum.

Softeners, emulsifiers and fillers may alternatively be added to the polymers as part of the gum base formulation.

The gum bases of Example 5 were used with the chewing gum formulations of Table 2 to prepare the following chewing gum samples:

Table 3: Chewing gum samples with different gum bases, enzyme concentrations and types of enzymes.

As shown in Table 3, each chewing gum sample was prepared with or without one of four different enzymes added in different amounts. Samples containing no enzyme were prepared as references. Applied enzymes were purchased from companies in Denmarac: Antra ApS (Bromelain, Bromelin), Novozymes (Neutrase and Trypsin, Product Name Neutrase 0.8L and Pancreatic Trypsin Novo 6.0S, without salt) and Danisco Cultor (glucose) Oxidase, trade name TS-E 760). Bromelain, Neutase and Glucose Oxidase were available as powders and trypsin as liquid.

Chewing gum products were prepared as follows:

The gum base was added to the mixing kettle with mixing means, for example horizontally placed Z-shaped arms. The chewing gum was prepared in one step immediately after the kettle was preheated to a temperature of about 60-80 ° C. for 15 minutes or after the gum base and the kettle were prepared in the same mixer having a temperature of about 60-80 ° C.

One half portion of sorbitol was added along with the gum base and mixed for 3 minutes. Thereafter, peppermint and menthol were added to the kettle and mixed for 1 minute. The other half portion of sorbitol was added and mixed for 1 minute.

Softeners were slowly added and mixed for 7 minutes. Aspartame and acesulfame were added to the kettle and mixed for 3 minutes. Xylitol was added to the kettle and mixed for 3 minutes. The enzyme was finally added and mixing continued for 1/2 minute. After the addition of the enzyme, care must be taken to ensure that the applied enzyme does not exceed the tolerable temperature. The resulting gum mixture was then drained and transferred to a pan, for example at a temperature of 40-48 ° C. The gum was then rolled up and cut into cores, sticks, cubes and other desired shapes, followed by coating and polishing prior to packaging or use. Obviously, within the scope of the present invention, other processes and components may be applied in the manufacture of the chewing gum, for example the one-step method may be a lenient alternative.

Example  7

Chewing  The decomposition of a sword

The chewing gum products prepared by Example 5 were chewed in a mastication device (CF Jansson) and left for degradation in air or phosphate buffer. Corresponding non-chewing chewing gum pieces were exposed to the same digestion. Both chewed gum and non-chewed chewing gum pieces were observed for 10 days and evaluated by visual rating and GC / MS-analysis.

Different kinds of chewing gum pieces according to Table 3 were individually exposed to the following experimental setups, and only 4 to 6 were applied to the unchewing gum pieces:

1. Place in a chewing apparatus containing 20 ml of phosphate buffer (0.02 M ammonium-di-hydrogen-phosphate adjusted to pH 7.4 with 2 M NaOH solution).

2. Chew for 5 minutes at a chewing frequency of 60 chewing / min.

3. Remove from solution to form a spherical ball.

4. Place in a centered Petri dish or in a closed glass container containing 5 ml (0.012M) phosphate buffer adjusted to pH 5.6.

5. Place the Petri dishes at 30 ° C., 70% relative humidity (RH) or place the glass with buffer solution at 30 ° C.

6. Evaluate degradation.

Evaluation process;

Visual evaluation:

The disassembly of each chewing gum piece was evaluated on two measures described below. Visual evaluation was performed after 3, 6 and 10 days.

The appearance of chewing gum in air or buffer was evaluated on a scale of 10 to 0:

10: No detectable decomposition.

9: modification from initial form; The chewing gum piece is therefore slightly open.

8: The chewing gum piece is much more open and loosened. In addition, initiation of disintegration takes place.

7: Cracking of the surface of the sword piece begins.

5: The surface of the sword piece is very cracked.

1: Chewing gum piece completely disintegrated and found as a suspension.

0: Chewing gum piece completely disassembled.

The appearance of the buffer solution containing the chewing gum pieces was evaluated on a scale of P1 to P10:

PO: No visible change in solution.

P1: Several small particles are formed but the solution appears transparent.

P3: The solution is relatively transparent, but contains several small flakes and / or several large “slimy” particles.

P6: The solution is very “slimey”, the number and size of flakes is increased and the transparency of the solution is reduced.

P10: The solution contains a full chewing gum operation in the form of small particles.

GC / MS Analysis:

The method used in the evaluation by GC / MS included headspace sampling (Perkin Elmer Turbo Matrix 40), so that after disassembly, the chewing gum residues and buffer solution were placed in vials and the component was released into the headspace. . After the period of equilibration, the sample of headspace-air was injected into the GC / MS-system (Perkin Elmer Clarus 500) and the areas of the relevant peaks in the resulting chromatogram were evaluated to determine the effect of the different treatments described in the following results section. Comparison was made as follows.

Visual evaluation result

The visual evaluation results of enzyme-containing chewing gum pieces (and reference gum pieces not containing enzymes) that were left for degradation are described below.

In the case of chewing gum that was left in the air, the change that could be detected with the naked eye was minimal. After 10 days, non-chewed gum pieces were given an overall disintegration score of 10, while chewed gum pieces were given a score of 9 because their spheres were deformed and some opening or loosening could be observed. In the case of chewing gum that was left in the buffer solution, the effect of the enzyme was more pronounced. For both chewed and unchewed gums, these experiments showed that in some cases the inclusion of enzymes in chewing gums had a facilitating effect on chewing gum degradation.

From Tables 4 and 5, the addition of enzymes appears to promote chewing gum degradation compared to enzyme free chewing gum. In addition, the effect of increasing enzyme concentration is increased degradation.

Chewing gum containing glucose oxidase behaves differently from the rest of the sample in that the enzyme effects showed different symptoms, ie, highly sticky for chewed gums and shrinking for unchewed gums. did.

It should also be noted that there is a difference in the visible degradation of chewing gums including gum bases 101 and 102, which means that the consequences of the effects of enzymes vary and depend on the type of polymer used. Different gum bases react in different ways to the addition of enzymes and it can be predicted that giving optimal degradation is determined by designing suitable combinations of polymers and enzymes. It may include both conventional polymers and polymers considered biodegradable.

Table 6 shows the results of pH measurements in buffer solutions performed after 10 days:

Table 6: pH of buffer solution after 10 days

Despite the buffers that were adjusted to pH 5.6 from Table 6, the pH in the solutions around the chewed or unchewed gums decreased, which seems to indicate the occurrence of degradation.

GC Of MS  Evaluation results

The results of the GC / MS-evaluation are provided in FIGS. 1-4, which illustrate the formation of two different compounds from chewing gum degradation. The charts relate to the following chewing gum numbers:

1 A and G,

2 A, F and I

3 A, E, H and J

4 A, B, C and D

Overall, the results confirm that chewing gums containing enzymes are distinguished from chewing gums containing no enzymes by the appearance of higher amounts of degradation products.

Figure 1 shows that Compound a, one of the degradation products, was formed in higher amounts as a result of the addition of the oxidoreductase glucose oxidase.

2A and 2B show that the formation of both degradation products was increased by increasing the amount of neutraase, the added hydrolase.

FIG. 3 shows that the decomposition product, Compound a, was formed in increased amounts by increasing the content of bromelain in the chewing gum. However, at the maximum content of enzyme, smaller amounts of degradation products were formed. This may be the result of an overload of enzymes. It can be expected that enzymatic activity can be hindered at enzyme concentrations above a certain optimal concentration, which means that it depends on designing a suitable relationship between polymer concentration and enzyme content in the chewing gum.

In FIG. 3B, an increase in bromelain enzyme concentration results in more formation of compound b, a degradation product, but an increase in degradation product between 15% and 45% enzyme concentration appears to be somewhat low. This in turn means that obtaining a catalyzed degradation is determined by providing a suitable level of enzyme concentration.

4A and 4B show the tendency to affect degradation, although the correlation is not clearly proportional when the concentration of trypsin enzyme in chewing gum is increased.

It is generally found that different kinds of enzymes can show the desired effect of degradation. In this test, both hydrolase and oxidoreductases affected degradation as a catalyst, which could be observed by naked eye and by GC / MS.

It should be noted overall that it is not clear that higher enzyme concentrations lead to faster degradation. The relationship between the polymer substrate and the enzyme should be optimized.

Claims (75)

Chewing gum comprising one or more polymers, chewing gum components and enzymes, wherein one or more of the polymers form a substrate for one or more of the enzymes. The chewing gum of claim 1, wherein the chewing gum comprises center filling. The chewing gum of claim 1 or 2, wherein the chewing gum comprises a coating. The chewing gum according to any one of claims 1 to 3, wherein the chewing gum ingredients comprise sweeteners and flavorings. 5. Chewing gum according to claim 1, wherein the chewing gum ingredients comprise softeners and other additives. 6. The method of claim 1, wherein the one or more polymers make up the chewing gum base. The chewing gum of claim 1, wherein the one or more polymers comprise one or more copolymers. The chewing gum of claim 1, wherein the one or more copolymers are polymerized of two or more different monomers, each constituting 1-99%. The chewing gum of claim 1, wherein the one or more polymers comprise one or more biodegradable polymers. 10. Chewing gum according to any one of the preceding claims, wherein at least one of the at least one biodegradable polymer comprises at least one biodegradable elastomer. The chewing gum of claim 1, wherein at least one of said at least one biodegradable polymer comprises at least one biodegradable elastomeric plasticizer. The chewing gum of claim 1, wherein at least one of said at least one biodegradable polymer comprises at least one polyester polymer obtained by the polymerization of at least one cyclic ester. The method of claim 1, wherein at least one of the at least one biodegradable polymer comprises at least one polyester polymer obtained by polymerization of at least one alcohol or derivative thereof with at least one acid or derivative thereof. Chewing gum that contains. 14. The compound according to any one of claims 1 to 13, wherein at least one of the at least one biodegradable polymer is selected from the group of cyclic esters, alcohols or derivatives thereof and carboxylic acids or derivatives thereof. Chewing gum comprising at least one polyester obtained by the polymerization of. 15. The method according to any one of claims 1 to 14, wherein the one or more polyesters obtained by the polymerization of one or more cyclic esters are at least partially derived from α-hydroxy acids, such as lactic and glycolic acids. In Chewing Gum. The method of claim 1, wherein the one or more polyesters obtained by polymerization of one or more cyclic esters are at least partially derived from α-hydroxy acids and the polyesters obtained are 20 Chewing gum comprising at least mole% α-hydroxy acid units, preferably at least 50 mole% α-hydroxy acid units and most preferably at least 80 mole% α-hydroxy acid units. . The chewing according to any one of claims 1 to 16, wherein the one or more cyclic esters are selected from the group of glycolides, lactides, lactones, cyclic carbonates or mixtures thereof. sword. 18. The lactone monomers according to claim 1, wherein the lactone monomers are selected from the group of ε-caprolactone, δ-valerolactone, γ-butyrolactone, and β-propiolactone, and are also the same carbon Ε-caprolactones, δ-valerolac, substituted with one or more alkyl or aryl substituents at non-carbonyl carbon atoms on the ring, including compounds containing two substituents on the atom Chewing gum which is selected from the group containing tons, (gamma) -butyrolactones, or (beta) -propiolactones. 19. The monomer of claim 1, wherein the carbonate monomer is trimethylene carbonate, 5-alkyl-1,3-dioxan-2-one, 5,5-dialkyl-1,3 -Dioxan-2-one, or 5-alkyl-5-alkyloxycarbonyl-1,3-dioxan-2-one, ethylene carbonate, 3-ethyl-3-hydroxymethyl, propylene carbonate Of trimethylolpropane monocarbonate, 4,6-dimethyl-1,3-propylene carbonate, 2,2-dimethyl trimethylene carbonate, and 1,3-dioxepan-2-one and mixtures thereof Chewing gum selected from the group. 20. The cyclic ester polymers and copolymers thereof according to any one of claims 1 to 19 obtained from the polymerization of cyclic ester monomers are poly (L-lactide); Poly (D-lactide); Poly (D, L-lactide); Poly (methoractide); Poly (glycolide); Poly (trimethylene carbonate); Poly (epsilon-caprolactone); Poly (L-lactide-co-D, L-lactide); Poly (L-lactide-co-meso-lactide); Poly (L-lactide-co-glycolide); Poly (L-lactide-co-trimethylenecarbonate); Poly (L-lactide-co-epsilon-caprolactone); Poly (D, L-lactide-co-meso-lactide); Poly (D, L-lactide-co-glycolide); Poly (D, L-lactide-co-trimethylenecarbonate); Poly (D, L-lactide-co-epsilon-caprolactone); Poly (meth-lactide-co-glycolide); Poly (metho-lactide-co-trimethylenecarbonate); Poly (metho-lactide-co-epsilon-caprolactone); Poly (glycolide-co-trimethylenecarbonate); Chewing gum comprising poly (glycolide-co-epsilon-caprolactone). The method of claim 1, wherein the one or more polymers have a crystallinity in the range of 0 to 95%, more preferably in the range of 0 to 70%. Chewing gum. 22. Chewing gum according to any one of the preceding claims, wherein at least one of the one or more polymers has amorphous regions. The chewing gum of claim 1, wherein the one or more polymers are aliphatic. 24. Chewing gum according to any of the preceding claims, wherein the molecular weight of the at least one polymer is in the range of 500-500000 g / mol, preferably in the range of 1500-200000 g / mol Mn. 25. Chewing gum according to any one of claims 1 to 24, wherein one or more of the enzymes catalyzes the degradation of the one or more polymers. 26. Chewing gum according to any one of claims 1 to 25, wherein after use the chewing gum disintegrates partially due to the influence of the enzymes. 27. Chewing gum according to any one of claims 1 to 26, wherein one or more of the enzymes affect the polymer substrate and as a result result in partial disintegration of the chewing gum. 28. Chewing gum according to any one of claims 1 to 27, wherein one or more of the enzymes affect the polymer substrate resulting in partial disintegration and crumbling structure of the chewing gum. 29. Chewing gum according to any one of the preceding claims, wherein after use of the chewing gum one or more of the enzymes catalyze the degradation of the polymer substrate until the one or more polymers are completely degraded. 30. Chewing gum according to any one of the preceding claims, wherein at least one said enzyme is active at atmospheric pressure and at its pressure and promotes degradation of said at least one polymer. 31. Chewing gum according to any of the preceding claims, wherein at least one of the enzymes is included in a chewing gum, gum base, center filling or coating. 32. The method of any one of the preceding claims, wherein at least one of the enzymes facilitates degradation of the polyester obtained by ring-opening polymerization of one or more cyclic esters. Chewing gum. 33. Chewing according to any one of the preceding claims, wherein at least one said enzyme promotes the degradation of said polyester obtained by the polymerization of at least one alcohol or derivative thereof with at least one acid or derivative thereof. sword. 34. The ring of any one of claims 1 to 33, wherein the chewing gum is obtained by the polymerization of one or more alcohols or derivatives thereof with one or more acids or derivatives thereof. Chewing gum comprising at least one polyester obtained by open polymerization. 35. The moisture content of any of claims 1 to 34, wherein the chewing gum is less than 10% by weight, preferably less than 5% by weight, more preferably less than 1% by weight and most preferably less than 0.1% by weight. Chewing gum having. 36. The chewing gum according to any one of claims 1 to 35, wherein the chewing gum is at least 0.1% by weight, preferably at least 5% by weight, more preferably at least 10% by weight, even more preferably at least 20% by weight and most Preferably chewing gum that can absorb water in an amount of at least 40% by weight. 37. Chewing gum according to any one of claims 1 to 36, wherein the chewing gum comprises filler in an amount of 0 to 80% by weight. 38. Chewing gum according to any one of the preceding claims, wherein the concentration of enzymes is in the range of 0.0001% to 50% by weight of the chewing gum. 39. Chewing gum according to any one of the preceding claims, wherein the concentration of enzymes is in the range of 0.001% to 10% by weight of the chewing gum. 40. Chewing gum according to any one of the preceding claims, wherein the concentration of enzymes is in the range of 0.01% to 5% by weight of the chewing gum. 41. Chewing gum according to any one of the preceding claims, wherein the amount of enzyme is in the range of 0.0001 to 80% by weight relative to the gum base amount of the chewing gum. 42. Chewing gum according to any one of claims 1 to 41, wherein the amount of enzyme is in the range of 0.001 to 40% by weight relative to the gum base amount of the chewing gum. 43. Chewing gum according to any one of claims 1 to 42, wherein the amount of enzyme is in the range of 0.1 to 20% by weight relative to the gum base amount of the chewing gum. The method according to any one of claims 1 to 43, wherein at least one of the enzymes consists of redox enzymes, transferases, hydrolases, lyases, isomerases and ligases. Chewing gum which is selected from the group which becomes. 45. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes are redox enzymes. 46. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes is a hydrolase. The chewing gum of any one of claims 1-46, wherein one or more of the enzymes are lyases. 48. Chewing gum according to any one of the preceding claims, wherein one or more of the hydrolase enzymes act on ester bonds. 49. Chewing gum according to any one of claims 1 to 48, wherein one or more of the hydrolase enzymes is glycosylase. 50. Chewing gum according to any of the preceding claims, wherein one or more of the hydrolase enzymes act on ether bonds. 51. Chewing gum according to any one of the preceding claims, wherein one or more of the hydrolase enzymes act on carbon-nitrogen bonds. 52. Chewing gum according to any one of the preceding claims, wherein one or more of the hydrolase enzymes act on peptide bonds. The chewing gum of claim 1, wherein one or more of the hydrolase enzymes act on acid anhydrides. 55. Chewing gum according to any one of the preceding claims, wherein one or more of the hydrolase enzymes act on carbon-carbon bonds. The method of claim 1, wherein one or more of the hydrolase enzymes are halide bonds, phosphorus-nitrogen bonds, sulfur-nitrogen bonds, carbon-phosphorus bonds, sulfur- Chewing gum that acts on sulfur bonds or carbon-sulfur bonds. The chewing gum of claim 1, wherein the one or more enzymes are selected from the group of lipases, esterases, dipolymerases, peptidases and proteases. The chewing gum of claim 1, wherein one or more of the enzymes is an endo-enzyme. 58. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes are exso-enzyme. 59. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes have a molecular weight of 2 to 1000 kDa, preferably 10 to 500 kDa. 60. Chewing gum according to any one of the preceding claims, wherein two or more of the enzymes are combined. 61. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes require a co-factor to carry out the catalysis. 62. Chewing gum according to any one of claims 1 to 61, wherein one or more of the enzymes are included in the chewing gum. 63. Chewing gum according to any one of the preceding claims, wherein one or more of the enzymes are included in the gum base. 64. Chewing gum according to any one of claims 1 to 63, wherein one or more of the enzymes are included in the coating. 65. The method according to any one of the preceding claims, wherein one or more of the enzymes exhibits optimal activity in a pH range of 1.0 to 11.0, preferably in a pH range of 4.0 to 8.0 and most preferably in a pH range of 4.0 to 6.0. Chewing gum that has. 66. The process of any one of the preceding claims, wherein one or more of the enzymes is in the temperature range of -10 to 60 ° C, preferably in the range of 0 to 50 ° C, more preferably in the range of 5 to 40 ° C. And most preferably having the optimum activity in the temperature range of 10 to 35 ° C. 67. Chewing gum according to any of the preceding claims, wherein one or more of the enzymes have optimal activity at relative humidity conditions in the range of 10 to 100% RH, preferably 30 to 100% RH. 68. Chewing gum according to any of the preceding claims, wherein the chewing gum is prepared by a one-step process. 70. Chewing gum according to any of the preceding claims, wherein the chewing gum is prepared by a two-step process. 70. Chewing gum according to any of claims 1 to 69, wherein the chewing gum is prepared by a continuous mixing process. 71. Chewing gum according to any of the preceding claims, wherein the chewing gum is compressed and manufactured by the use of compression techniques. Use for the degradation of biodegradable chewing gum of one or more enzymes. 73. The use of claim 72, wherein the one or more enzymes comprise hydrolases. A method of degradation of biodegradable chewing gum, wherein the one or more biodegradable polymers are at least partially degraded by one or more enzymes. 75. The method of claim 74, wherein the enzyme is mixed with the one or more biodegradable polymers by chewing.

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