WO2001001788A1 - Gomme a macher ingerable et degradable renfermant des hydrolysats enzymatiques de proteines - Google Patents
Gomme a macher ingerable et degradable renfermant des hydrolysats enzymatiques de proteines Download PDFInfo
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- WO2001001788A1 WO2001001788A1 PCT/US2000/007809 US0007809W WO0101788A1 WO 2001001788 A1 WO2001001788 A1 WO 2001001788A1 US 0007809 W US0007809 W US 0007809W WO 0101788 A1 WO0101788 A1 WO 0101788A1
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- Prior art keywords
- gum
- zein
- gum base
- chewing gum
- chewing
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Classifications
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G4/00—Chewing gum
- A23G4/06—Chewing gum characterised by the composition containing organic or inorganic compounds
- A23G4/14—Chewing gum characterised by the composition containing organic or inorganic compounds containing peptides or proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G4/00—Chewing gum
- A23G4/06—Chewing gum characterised by the composition containing organic or inorganic compounds
- A23G4/066—Chewing gum characterised by the composition containing organic or inorganic compounds characterised by the fat used
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G4/00—Chewing gum
- A23G4/06—Chewing gum characterised by the composition containing organic or inorganic compounds
- A23G4/08—Chewing gum characterised by the composition containing organic or inorganic compounds of the chewing gum base
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
Definitions
- the present invention relates generally to chewing gum and the manufacture of same. More specifically, the present invention relates to chewing gum bases and methods and materials for manufacturing same.
- typically ingestible polymers such as proteins and polysaccharides
- plasticizers such as water, alcohol, and glycerin or polyols
- some proteins and polysaccharides become elastic at body temperature.
- some other ingestible polymers such as starches, albumins, globulins, due to their polar structures, have a tendency to quickly dissolve or disperse in the mouth of the chewer. Such ingestible polymers therefore cannot stand up to prolonged chewing.
- Water insoluble ingestible polymers such as prolamines and glutelins have been explored for formulating ingestible chewing gums.
- prolamine solvents such as alcohol and polyol are still water-soluble or dispersable in water. They therefore can be extracted out during chewing.
- Chewing gums comprising prolamines as well as zein have been used or proposed. See, for example, U.S. Patent Nos. 2,154,482, 2,469,861, 2,489,147, 5,482,722 and 5,112,625. However, these products have not been entirely satisfactory from a chewing gum standpoint.
- the present invention provides improved chewing gum and gum bases.
- the improved chewing gum and gum bases are ingestible and/or biodegradable.
- the present invention provides a gum base comprising enzymatically hydrolyzed zein.
- the zein is hydrolyzed with a peptidase.
- the zein is hydrolyzed with a proteinase.
- the gum base includes a humectant. In an embodiment, the gum base includes an emulsifier.
- the gum base includes a polysaccharide.
- the gum base includes an ingestible protein.
- the gum base includes a lipid.
- the enzymatically hydrolyzed zein comprises approximately 0% to about 65% percent by weight of the gum base.
- the gum base includes an edible acid.
- a gum base comprising an enzymatically hydrolyzed protein and a polysaccharide.
- a chewing gum comprises an insoluble gum base including enzymatically hydrolyzed zein and a water soluble portion including a flavor and a sweetener.
- the zein is hydrolyzed with a peptidase.
- the zein is hydrolyzed with a proteinase.
- the chewing gum includes a humectant.
- the chewing gum includes an emulsifier.
- the chewing gum includes a polysaccharide.
- the chewing gum includes an ingestible protein. In an embodiment, the chewing gum includes a lipid.
- the enzymatically hydrolyzed zein comprises approximately 20% to about 65% percent by weight of the chewing gum base. In an embodiment, the zein is derived from corn.
- the chewing gum includes malt.
- a method for manufacturing a chewing gum comprises the steps of hydrolyzing zein using an enzyme and using the enzymatically hydrolyzed zein to produce a gum base.
- a method for manufacturing chewing gum comprises the steps of providing a gum base including an enzymatically hydrolyzed zein; and mixing with the gum base a flavor and a sweetener to provide a finished chewing gum.
- the finished chewing gum is heated. Accordingly, it is an advantage of the present invention to provide an improved chewing gum.
- Another advantage of the present invention is to provide an improved gum base.
- Still another advantage of the present invention is to provide a gum cud that is ingestible. Furthermore, an advantage of the present invention is to provide a chewing gum that produces a gum cud that does not cause environmental concerns if improperly discarded.
- an advantage of the present invention is to provide new ingredients for constructing gum bases.
- Another advantage of the present invention is to provide improved elastomers for constructing chewing gum.
- Still an advantage of the present invention is to provide an improved method for manufacturing chewing gum.
- FIGURE 1 illustrates graphically carbon conversation versus biodegradation over time (days) for Kraft paper, cellulose, and enzymatic zein gum base.
- the present invention provides improved chewing gum, improved gum bases, and methods of manufacturing same.
- an enzymatic hydrolysate of protein is used to construct chewing gum.
- an enzymatic hydrolsate of zein is used. This affords a gum base, or chewing gum, having a number of advantages.
- One of the essential requirements for a chewable material is that its glass transition temperature should not be higher than the temperature of the mouth of the chewer. It is well known that water is an important plasticizer for most food polymers. Water decreases the glass transition temperature of most biological materials from about
- Human saliva consists mainly of water and can be a plasticizer for food polymers during chewing.
- the water absorbing capacity is usually too high or is unlimited. This results in the dissolution or dispersion of the food polymers inside the mouth. Therefore, such products can not withstand prolonged chewing.
- hydrophobic food polymers such as zein
- Zein is composed of more than 50% nonpolar amino acid residuals such as leucine, isoleucine, valine, alanine, proline, and glutamine. This renders zein primarily soluble in alcoholic solvents and insoluble in water. Chemically intact zein has a moisture absorption capacity of less than 20%. In order to make a lipid-free ingestible chewing gum with zein one must balance its water retention ability and water solubility.
- tackifiers play an important role in balancing deformation and cohesion.
- low and medium molecular weight ingredients other than plasticizers are also required for ingestible gum.
- an enzymatic hydrolysate of zein is used to overcome these two problems.
- a significant improvement in solubility and foaming properties of zein is achieved.
- Enzymatic modification of zein exposes ionizable polar amino acids. These amino acids are capable of binding much more water than the nonionized polar groups in the intact zein.
- the water absorption capacity of zein hydrolysate can be 10 times higher than that of normal zein.
- a desired water holding ability can be obtained.
- the enzymatic hydrolysates of the proteins results in a softer texture than its original form in a water-rich environment, such as the mouth.
- zein has an average molecular weight of around 35,000 Dalton. After modification by proteases, such as papain, a hydrolysate having a molecular weight around 3,700 to about 5,400 Daltons can be produced. A zein product containing a certain amount of hydrolysate and water becomes quite chewable.
- a protein backbone is not very reactive chemically.
- a peptide bond is hydrolyzed very slowly at neutral pH and room temperature.
- the process can be greatly accelerated.
- enzymes including microbial (fungal or bacterial) proteases, plant extracted proteases, and their combinations can be used.
- the proteases are endopeptidase; most preferably serine proteases or thio proteases or their combinations.
- proteins can be hydrolyzed by different types of proteases.
- the proteases that can catalyze the hydrolysis of protein can be divided into two categories: peptidase (exopeptidases); and proteinases (endopeptidases).
- Exopeptidases catalyze the hydrolysis of the N-terminal and C-terminal ends of proteins.
- Endopeptidases catalyze the hydrolysis of peptide bonds within the protein chain.
- proteases can be subdivided into serine proteinases, thio or cysteine proteinases, carboxyl or aspartic proteinases and metalloproteinases.
- proteases that can be used in the present invention include: the peptidase Validase FP II (obtained from Valley Research, Inc.) that contains a very high level of exopeptide; the proteinases Alcalase (obtained from Novo Nordisk BioChem North America, Inc.); Alkaline Protease (a bacterial protease liquid concentrate obtained from a non-genetically modified strain of Bacillus licheniformis (660DAPU/g) obtained from Valley Research Inc.; Validase TSP200 (obtained from Valley Research, Inc.), Protamex (obtained from Novo Nordisk BioChem North America, Inc.) and Neutrase (obtained from Novo Nordisk BioChem North America, Inc.) that are characterized primarily by their endopeptidase activities; Flavourzyme (obtained from Novo Nordisk BioChem North America, Inc.) contains both endopeptidase and exopeptidase.
- Serine proteinases are characterized by the presence of unique serine hydroxyl groups on the side chain in each enzyme.
- serine proteases There are two families of serine proteases: bacterial protease subtilisin; and trypsin family including chymotrypsin, trypsin, elastase, thrombin, plasmin, kallikrein and acrosin.
- bacterial protease subtilisin subtilisin
- trypsin family including chymotrypsin, trypsin, elastase, thrombin, plasmin, kallikrein and acrosin.
- Various serine proteases catalyze the hydrolysis reaction in very similar manners but, are different in their preferences for amino acid side chains at the cleaved peptide bonds and the residuals at the neighboring position. All highly purified proteases demonstrated specificity for certain peptide bonds and have little or no action on other peptide bonds.
- subtilisin because chymotrypsin prefers to cleave the bonds after large hydrophobic residuals, it should be suitable for the zein hydrolysis.
- the subtilisin family has less distinct preferences at the residual on the cleaved peptide bond. It was found that the texture of zein treated by a subtilisin was soft and chewable. The resultant hydrolysates can be used as a chewing gum material.
- thiol protease the cysteine side chain is the active site.
- Papain, ficin, bromelain and actinidin are typical thiol proteases. When trace amount of papain was mixed with zein in a humectant for 2.5 hours at 56°C, the partially hydrolyzed zein became much softer than one without papain, as shown in Table 1.
- *moduli are measured from a punch test by use of a texture analyzer.
- carboxyl proteases the carboxyl group, usually aspartyl, is the active site for catalyzing hydrolysis of proteins.
- proteases include pepsin, gastricsin and chymosin.
- the texture of zein can be modified by pepsin.
- Metalloproteases employ bonded metals, such as Zn* "1" and Ca 4 ⁇ in their active sites.
- Carboxypeptidases A and B thermolysin, angiotensin-converting enzyme, enkephalinase, collagenase (Zn ⁇ ) are examples of metalloproteases.
- Neutrase a metalloproteinase (Zn) produced by a selected strain of Bacillus amyloliquefaciens, was used to treat zein, the hydrolsate was firmer than the one treated by subtilisin or papain.
- Alkaline Protease Concentrate a bacterial protease liquid obtained from a non- genetically modified strain of Bacillus licheniformis (660DAPU/g) is an example of a protease complex.
- zein was treated by trace amount of Alkaline Protease
- the degree of hydrolysis and the structure of the peptides produced determines the properties of a protein hydrolsate. This in turn is dependent on the nature of the protein and the specificity of the enzyme used, as well as the hydrolysis conditions such as pH and temperature, time and solvents. Due to the hydrophobic nature of zein, a homogeneous enzymatic hydrolysis of zein is very difficult to perform under the conditions for water-soluble proteins. For example, when the papain-catalyzed hydrolysis of zein was carried out in a homogeneous 70%) ethanol solution, zein was hydrolyzed to a limited extent and the hydrolysates had a considerably higher molecular weight compared to the products obtained in a suspension system. Fortunately, it has also been found that zein hydrolysates with a degree of hydrolysis less than 2% contained many components in different sizes. The mixtures of polypeptides had substantially increased solubility even with such a low degree of hydrolysis.
- the enzymatic zein of the present invention can be used as a mastication material alone in the presence of water and with other humectants. It can also be combined with other ingestible ingredients to make ingestible gum bases having improved taste and texture.
- Other ingestible ingredients include, but are not limited to one or more of the following materials: polysaccharides; proteins or their hydrolysates; ingestible acids; emulsifiers; and lipids.
- Polysaccharides include, but are not limited to: native starches; modified starches; dextrins; maltodextrin; hydroxypropylmethylcellulose; dietary fibers; pectins; alginates; carrageenan; gellan gum; xanthan gum; gum arabic; and guar gum or other natural gums.
- the preferred polysaccharides are maltodextrin and high-conversion dextrins.
- the chewing gum bases comprise approximately
- polysaccharides 5 to about 10% (wt.) polysaccharides.
- digestible proteins hydrolyzed collagens or gelatins can be used.
- gelatins can also be used in the gum base.
- the preferred content of gelatin is around 10 to about 20% (wt.) of the base.
- other protein hydrolysates for example gelatin hydrolsate, hydrocolloids such as guar flour, pectin, maltodextrin and acids one can reduce any bitter taste that may be present in the enzymatic zein.
- High molecular weight hydrolyzed gelatin can also decrease the adhesive force and increase the springiness of the gums.
- starches and dextrin can increase the sugar-holding capacity of the gum bases.
- an ingestible and chewable gum base is provided that is derived from the enzymatic hydrolysate of corn proteins.
- the corn proteins comprise mainly zein.
- a method for preparing ingestible and chewable enzymatic hydrolsate of zein is also provided.
- the method of this invention can, but not necessarily, involve the blending of zein, an enzyme and humectant in a batch mixer. This can be done at approximately 20°C to about 65°C for approximately 1 to about 2 hours. In a preferred embodiment, the process is performed at a temperature of approximately 45 C C to about 60°C.
- the method comprises blending enzymatic zein, polysaccharides, proteins and/or fats with emulsifiers. This can be done at approximately 20°C to about 65°C, preferably at approximately 35 °C to about 45°C for approximately 1 hour.
- sugarless, ingestible chewing gums comprising enzymatic hydrolsate of zein, one or more high-intensity sweeteners, flavors and in a preferred embodiment, bitterness masking agents.
- the high- intensity sweeteners can include aspartame, alitame, acesulfame, acesulfame salt, sucralose, saccharin, cyclamic acid, thaumatin, monellin, glycyrrhizin, dihydrochalcones and stevioside; the preferred amount of high-intensity sweeteners is approximately 0.5 to about 2% in the finished gum.
- the enzymatic zein gums can comprise approximately 0.5 to about 2% (wt.) flavors such as strawberry, spearmint, vanilla, etc.
- the preferred bitterness masking agent is malt with a preferred content of approximately 5 to about 50%(wt.) in the fimshed gums.
- the ingestible chewing gums comprise one of the gum bases described above, one or more flavors, preferably one or more bitterness masking agents, one or more sugars and/or one or more high-intensity sweeteners.
- Sugars can include monosaccharides, disaccharides and/or oligosaccharides such as sucrose, dextrose, maltose, fructose, levulose, galactose and their combinations.
- a sugar content of approximately 30 to about 50%(wt.) is provided in the finished chewing gum.
- the finished chewing gum is heated at an elevated temperature for a short period of time.
- the preferred conditions are approximately 90 °C to about 110 ° C for approximately 3 to about 20 minutes in a closed system.
- the humectants that can be used include aqueous glycols, polyols or alcohols.
- aqueous propylene glycol is used.
- the water content in the humectants should be approximately 5 to about 60%), preferably approximately 30 to about 60%, and most preferably, approximately 40 to about 60% by weight. The higher the water content in the humectants, the better the taste of the hydrolysates.
- the protein to humectant ratio should be approximately 0.2 to about 3.0, preferably approximately 0.5 to about 2, and most preferably approximately 1 to about 1.5.
- the peptide bonds cleaved during hydrolysis may form sub-units that react with other proteins or non-proteins.
- the content of free amino acids or the residuals with amine or carboxyl side chains will increase with an increase of the hydrolysis degree.
- the pH value of the entire system tends to decrease in the absence of a buffer solution.
- the buffer can help to achieve a hydrolysis degree (HD) of the hydrolysates. Gum-grade hydrolysate can be prepared with or without buffer.
- Table 2 (below) illustrates hydrolysis time versus the degree of hydrolysis. After a one-hour hydrolysis, zein became soft and chewable with HD around 1.8%. Table 2. Hydrolysis time vs. hydrolysis degree
- Table 3 (below) sets forth the ratio of protein to enzyme versus the modulus of the gum.
- the ratio of protein to enzyme also greatly affected the texture of the hydrolysate. With an increase of papain content, the modulus decreased.
- the papain/zein ratio was perhaps the most significant factor on the gum texture, such as hardness, modulus, gumminess, chewiness and springiness; it also had some impact on cohesiveness and adhesive force. Table 3 demonstrates that the higher the papain/zein ratio the softer the gum.
- the enzymatic zein gum base will be biodegradable.
- zein When zein was exposed to aerobic biodegradation pursuant to ASTM D-5209 by contacting with activated sewage sludge innoculum, its degradation rate was faster than both Kraft paper and cellulose as illustrated in Figure 1. The weight loss was 100% after about 80 days in sewage sludge. This indicated that zein would degrade completely in less than three months.
- the present invention can be used to construct a variety of chewing gums.
- the chewing gum includes a base portion.
- a variety of ingredients can be used with zein to construct the gum base.
- a gum base Preferably as a gum base one or more of the following ingredients is added to the hydrolysate.
- Edible proteins such as, but not limited to, gelatin, collagen, casein, casemates, gliadin, gluten, glutenin, hordein and their combinations can be used.
- Protein hydrolysates such as but not limited to hydrolyzed gelatin, hydrolyzed collagen, hydrolyzed gluten may also be used alone or in combination.
- Food grade microbial (fungal or bacterial) proteases or plant protease extracts which contain thiol proteinases, or serine proteinases, or carboxyl proteinases, or metalloproteinases or their combinations such as but not limited to subtilisin, chymotrypsin, trypsin, elastase, thrombin, plasmin, kallikrein, acrosin, papain, f ⁇ cin, bromelain, actinidin, pepsin, gastricsin, chymosin, carboxypeptidases A and B, thermolysin, enkephalinase, collagenase.
- Humectant such as, but not limited to, aqueous glycol, polyol, alcohol or their combinations such as water, propylene glycol, glycerin, polyethylene glycol, ethanol, propanol may also be used in the base.
- Food grade polysaccharides such as, but not limited to, native starches, modified starches, dextrins, maltodextrin, hydroxyethylcellulose, hydroxypropylcellulose, dietary fibers, pectins, alginates, carrageenan, gellan gum, xanthan gum, gum arabic, guar gum or other natural gums may be used in the base; the preferred polysaccharides are maltodextrin and high-conversion dextrins.
- Bitterness masking agents such as, but not limited to, malt, anethole, gelatin hydrolysate, guar flour, pectin, maltodextrin, sodium salts, lithium salts, phosphatidic acid, phosphatidyl inositol, ribonucleotide, acidic oligopecptides, lipoproteins and their combinations may also be used in the base.
- Ingestible minerals such as, but not limited to, calcium carbonate, calcium citrate, calcium lactate may also be used in the base.
- Ingestible materials such as, but not limited to, beeswax, candilliba wax may also be used in the base.
- Edible fats such as, but not limited to, soya, cotton seed oil, palm oil, corn oil, peanut oil, cocoa butter and their hydrogenates may also be used in the base.
- Edible acids such as, but not limited to, citric acid, fumaric acid, lactic acid, malic acid, tartaric acid, ascoribc acid, sorbic acid, succinic acid and its anhydride, adipic acid, propionic acid may also be used in the base.
- Emulsifier such as, but not limited to, monoglycerides, diglycerides, propylene glycol ester, lactoglycerides, succinylated monoglycerides, acetoglycerides, sorbitan ester, polyglcerol esters, citroglycerides, polysorbates, polyglycerol polyricinoleate may also be used in the base.
- the zein hydrolysate comprises approximately 25% to about 55% by weight of the gum base.
- Gum formulas may comprise from about 10 to about 95 weight percent a gum base made in accordance with the present invention in a gum formula typically known to those in the art.
- the chewing gum may comprise softeners, sweeteners, flavoring agents and combinations thereof.
- the sweeteners often fill the role of bulking agents in the gum.
- the bulking agents generally comprise from about 5 percent to about 90 percent, preferably from about 20 percent to about 80 percent.
- Softeners are added to the chewing gum in order to optimize the chewability and mouth feel of the gum. Softeners typically constitute from about 0.5 percent to about 25.0 percent by weight of the chewing gum. Softeners contemplated for use in the gum include glycerin, lecithin and combinations thereof. Further, aqueous sweetener solutions such as those containing sorbitol, hydrogenated starch hydrolysates, corn syrup and combinations thereof may be used as softeners and bulking agents in gum. Sugar-free formulations are also typical.
- Sugar sweeteners generally include saccharide-containing components commonly known in the chewing gum art which comprise, but are not limited to, sucrose, dextrose, maltose, dextrin, dried invert sugar, fructose, levulose, galactose, corn syrup solids and the like, alone or in any combination.
- sugarless sweeteners include components with sweetening characteristics but which are devoid of the commonly known sugars and comprise, but are not limited to, sugar alcohols such as sorbitol, mannitol, xylitol, hydrogenated starch hydrolysates, maltitol and the like, alone or in any combination.
- bulk sweeteners of the present invention can also be used in combination with coated or uncoated high-intensity sweeteners or with high-intensity sweeteners coated with other materials and by other techniques.
- High-intensity sweeteners typically may include, but are not limited to, alitame, thaumatin, aspartame, sucralose, acesulfame, saccharin and dihydrochalcones.
- the range of these sweetener types in gum typically may range from about 0.02 to about 0.10 weight percent for sweeteners such as alitame, thaumatin and dihydrochalcones, and from about 0.1 to about 0.3 weight percent for sweeteners like aspartame, sucralose, acesulfame and saccharin.
- a flavoring agent may be present in the chewing gum in an amount within the range of from about 0.1 to about 10.0 weight percent and preferably from about 0.5 to about 3.0 weight percent of the gum.
- the flavoring agents may comprise essential oils, synthetic flavors, or mixtures thereof including, but not limited to, oils derived from plants and fruits such as citrus oils, fruit essences, peppermint oil, spearmint oil, clove oil, oil of wintergreen, anise and the like.
- Artificial flavoring components are also contemplated for use in gums of the present invention. Those skilled in the art will recognize that natural and artificial flavoring agents may be combined in any sensory acceptable blend. All such flavors and flavor blends are contemplated for use in gums of the present invention.
- Optional ingredients such as colors, emulsifiers and pharmaceutical agents may be added to the chewing gum.
- chewing gum is manufactured by sequentially adding the various chewing gum ingredients to a commercially available mixer known in the art. After the initial ingredients have been thoroughly mixed, the gum mass is discharged from the mixer and shaped into the desired form such as by rolling into sheets and cutting into sticks, extruded into chunks or casting into pellets.
- the ingredients are mixed by first melting the gum base and adding it to the running mixer. The base may also be melted in the mixer itself. Color or emulsifiers may also be added at this time. A softener such as glycerin may also be added at this time, along with syrup and a portion of the bulking agent/sweetener. Further portions of the bulking agent/sweetener may then be added to the mixer.
- a flavoring agent is typically added with the final portion of the bulking agent/sweetener.
- a high-intensity sweetener is preferably added after the final portion of bulking agent and flavor have been added.
- Example 1 Preparation of zein hydrolysate by enzyme complex: A propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 1 :1 by weight. Alkaline Protease Concentrate (APC, 0.25 grams) was then added into the PG aqueous solution (25 grams). To a 100-ml sigma-blade mixer, set at 60°C and 30 rpm, the zein (25 grams) and APC solution was added. After one hour of mixing, a homogenous, syrup-like paste was obtained. The paste was cooled to room temperature, and 0.5 g citric acid was added to deactivate the enzyme. The soft paste was then ready to be used for preparing the gums.
- PG propylene glycol
- APC Alkaline Protease Concentrate
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight.
- Liquid papain dried latex from papaya fruit, 165 MCU/mg,
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight.
- Alcalase 2.4 AU/g, 0.25 grams
- the main component in Alcalase is subtilisin carlsberg from the selected strain of Bacillus licheniformis.
- zein 25 grams
- the enzyme was inactivated for 10 minutes at 85°C before discharge. The soft paste was ready for preparing the gums.
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight.
- Neutrase 0.5 AU/g, 1.0 grams
- PG aqueous solution 25 grams
- Neutrase 0.5 AU/g
- zein 25 grams
- Example 5 Preparation of zein hydrolysate by exopetidase: The propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight. Validase FP II (50,000 CFAU/g, 0.25 grams) was then added into the PG aqueous solution (25 grams). Validase FP II (50,000 CFAU/g) is an exo-peptidase produced by the controlled fermentation of Aspergillus oryzae. To a 100- ml sigma-blade mixer, set at 53°C and 30 rpm speed, zein (25 grams) and the above Validase FP II solution were added. After two and a half hours of mixing, the blend was discharged. It was chewable, but firmer than the hydrolysate from example 1.
- Example 6 Preparation of zein hydrolysate by an endopeptidase:
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight.
- Validase TSP200 (200NU/g, 0.25 grams) was then added into the PG aqueous solution (25 grams).
- Validase TSP200 (200NU/g) is an endopeptidase produced by the controlled fermentation of Bacillus subtilis.
- zein 25 grams
- the above Validase TSP200 solution were added. After two and a half hours of mixing, the blend was discharged. It was chewable, but firmer than the hydrolysate from example 1.
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3 :2 by weight.
- Protamex 1.5 AU/g, 0.25 grams was then added into the PG aqueous solution.
- Protamex (1.5 AU/g) is a bacterial protease complex produced by the controlled fermentation o ⁇ Bacillus.
- zein 25 grams was added to a 100-ml sigma-blade mixer, set at 40°C and 30 rpm. After two and a half hours of mixing, the blend was discharged. It was chewable, but firmer than the hydrolysate from example 1.
- Example 8 Preparation of zein hydrolysate by protease complex: A propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 3:2 by weight. Flavourzyme (1000 LAPU/g, 0.25 grams) was then added into 25 ml of the PG aqueous solution. Flavourzyme (1000 LAPU/g) is a fungal protease complex produced by the fermentation of a selected strain of Aspergillus oryzae. To a 100-ml sigma-blade mixer, set at 50°C and 30 rpm, zein (25 grams) and the above Flavourzyme solution were added. After two and a half hour mixing, phase separation occurred.
- PG propylene glycol
- hydrolysates prepared pursuant to examples 1-3 50 grams
- maltodextrin 5 grams
- citric acid 0.5 grams
- a propylene glycol (PG) aqueous solution was prepared by mixing PG and water at a ratio of 1 : 1 by weight.
- Alkaline Protease Concentrate APC, 0.25 grams was then added into 17 ml of PG aqueous solution.
- zein 25 grams and the above APC solution were added.
- malt powder 10 grams was added and mixed for 40 minutes.
- the mixer was set at 37°C and 60 rpm.
- Acesulfame K (0.5 grams) and strawberry flavor (0.5 ml) were added and mixed for another 10 minutes before discharge.
- Example No. 9 63 grams
- malt powder 10 grams
- acesulfame K 0.5 grams
- strawberry flavor 0.5 ml
- Example No. 10 To a 100-ml sigma-blade mixer at 60°C and 60 rpm, the base prepared in Example No. 10 (63 grams), sugar(30 grams) and malt powder (10 grams) were added and mixed for 5 minutes. Then the mixer was re-set to 37°C and the blend was mixed for another 40 minutes. Then, acesulfame K (0.5 grams) and strawberry flavor (0.5 ml) were added and mixed for another 10 minutes.
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Inorganic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Nutrition Science (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Confectionery (AREA)
Abstract
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP00918332A EP1246539A4 (fr) | 1999-06-30 | 2000-03-24 | Gomme a macher ingerable et degradable renfermant des hydrolysats enzymatiques de proteines |
AU39161/00A AU775784B2 (en) | 1999-06-30 | 2000-03-24 | Ingestible and degradable chewing gum including enzymatic hydrolysates of proteins |
CA002373850A CA2373850C (fr) | 1999-06-30 | 2000-03-24 | Gomme a macher ingerable et degradable renfermant des hydrolysats enzymatiques de proteines |
US10/018,820 US6773730B1 (en) | 1999-06-30 | 2000-11-09 | Ingestible and degradable chewing gum including enzymatic hydrolysates of proteins |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US14160399P | 1999-06-30 | 1999-06-30 | |
US60/141,603 | 1999-06-30 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO2001001788A1 true WO2001001788A1 (fr) | 2001-01-11 |
Family
ID=22496397
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/US2000/007809 WO2001001788A1 (fr) | 1999-06-30 | 2000-03-24 | Gomme a macher ingerable et degradable renfermant des hydrolysats enzymatiques de proteines |
Country Status (5)
Country | Link |
---|---|
EP (1) | EP1246539A4 (fr) |
CN (1) | CN1145421C (fr) |
AU (1) | AU775784B2 (fr) |
CA (1) | CA2373850C (fr) |
WO (1) | WO2001001788A1 (fr) |
Cited By (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2001067883A1 (fr) * | 2000-03-17 | 2001-09-20 | Societe Des Produits Nestle S.A. | Chewing gum digestible |
WO2002076227A1 (fr) * | 2001-03-23 | 2002-10-03 | Gumlink A/S | Chewing-gum enrobe degradable a duree de vie prolongee et ses procedes de preparation |
ES2190875A1 (es) * | 2001-06-12 | 2003-08-16 | Cafosa Gum S A | Goma base degradable y los chicles obtenidos con las mismas. |
WO2005063037A1 (fr) * | 2003-12-30 | 2005-07-14 | Gumlink A/S | Gomme a macher comprenant des polymeres biodegradables et ayant une degradabilite acceleree |
EP1922937A2 (fr) | 2001-03-23 | 2008-05-21 | Gumlink A/S | Gomme à mâcher enrobée dégradable dotée d'une durée de vie améliorée et son procédé de fabrication. |
EP1994834A1 (fr) * | 2002-09-24 | 2008-11-26 | Gumlink A/S | Gomme à mâcher à faible humidité |
WO2010053908A1 (fr) * | 2008-11-06 | 2010-05-14 | Allison Flynn | Bases de gomme à mâcher biodégradables et leurs utilisations |
US7833555B2 (en) | 2002-09-24 | 2010-11-16 | Gumlink A/S | Chewing gum comprising at least two different biodegradable polymers |
US8591967B2 (en) | 2002-09-24 | 2013-11-26 | Gumlink A/S | Biodegradable chewing gum comprising at least one high molecular weight biodegradable polymer |
US9974320B2 (en) | 2011-11-07 | 2018-05-22 | Wm. Wrigley Jr. Company | Chewing gum base containing substituted polysaccharides and chewing gum products made there from |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8263143B2 (en) | 2005-08-22 | 2012-09-11 | Kraft Foods Global Brands Llc | Degradable chewing gum |
CN101312654B (zh) * | 2005-11-18 | 2011-07-20 | 吉百利亚当斯美国有限责任公司 | 可降解的咀嚼型胶基糖 |
CN105580968A (zh) * | 2015-12-17 | 2016-05-18 | 广州合诚实业有限公司 | 一种高胶原蛋白肽含量的无糖口香糖及其制备方法 |
CN110477178B (zh) * | 2019-08-22 | 2022-08-16 | 海南绿康安健康生物科技有限公司 | 蛋白核小球藻胶原蛋白肽凝胶糖果及其制备方法 |
Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US2154482A (en) * | 1937-01-30 | 1939-04-18 | Prolamine Products Inc | Chewing gum base |
US2469861A (en) * | 1946-03-02 | 1949-05-10 | American Chicle Co | Chewing gum base |
US2489147A (en) * | 1944-07-19 | 1949-11-22 | Boris N Lougovoy | Chewing gum base |
US5112625A (en) * | 1989-02-15 | 1992-05-12 | Wm. Wrigley Jr. Company | Aqueous zein coated sweeteners and other ingredients for chewing gum |
US5482722A (en) * | 1994-09-26 | 1996-01-09 | Opta Food Ingredients, Inc. | Confections comprising a proteinaceous chewable base |
US5624906A (en) * | 1994-12-08 | 1997-04-29 | Lever Brothers Company, Division Of Conopco, Inc. | Oral hygiene compositions comprising heteroatom containing alkyl aldonamide compounds |
US5741773A (en) * | 1996-04-26 | 1998-04-21 | Colgate Palmolive Company | Storage stable dentifrice composition containing an antibacterial casein glycomacropeptide adjuvant |
-
2000
- 2000-03-24 CN CNB008098476A patent/CN1145421C/zh not_active Expired - Fee Related
- 2000-03-24 CA CA002373850A patent/CA2373850C/fr not_active Expired - Fee Related
- 2000-03-24 EP EP00918332A patent/EP1246539A4/fr not_active Withdrawn
- 2000-03-24 WO PCT/US2000/007809 patent/WO2001001788A1/fr not_active Application Discontinuation
- 2000-03-24 AU AU39161/00A patent/AU775784B2/en not_active Ceased
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US2154482A (en) * | 1937-01-30 | 1939-04-18 | Prolamine Products Inc | Chewing gum base |
US2489147A (en) * | 1944-07-19 | 1949-11-22 | Boris N Lougovoy | Chewing gum base |
US2469861A (en) * | 1946-03-02 | 1949-05-10 | American Chicle Co | Chewing gum base |
US5112625A (en) * | 1989-02-15 | 1992-05-12 | Wm. Wrigley Jr. Company | Aqueous zein coated sweeteners and other ingredients for chewing gum |
US5482722A (en) * | 1994-09-26 | 1996-01-09 | Opta Food Ingredients, Inc. | Confections comprising a proteinaceous chewable base |
US5624906A (en) * | 1994-12-08 | 1997-04-29 | Lever Brothers Company, Division Of Conopco, Inc. | Oral hygiene compositions comprising heteroatom containing alkyl aldonamide compounds |
US5741773A (en) * | 1996-04-26 | 1998-04-21 | Colgate Palmolive Company | Storage stable dentifrice composition containing an antibacterial casein glycomacropeptide adjuvant |
Non-Patent Citations (1)
Title |
---|
See also references of EP1246539A4 * |
Cited By (14)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6872410B2 (en) | 2000-03-17 | 2005-03-29 | Nestec S.A. | Edible chewing gum and process for preparing |
WO2001067883A1 (fr) * | 2000-03-17 | 2001-09-20 | Societe Des Produits Nestle S.A. | Chewing gum digestible |
EP1922937A3 (fr) * | 2001-03-23 | 2008-06-04 | Gumlink A/S | Gomme à mâcher enrobée dégradable dotée d'une durée de vie améliorée et son procédé de fabrication. |
EP1922937A2 (fr) | 2001-03-23 | 2008-05-21 | Gumlink A/S | Gomme à mâcher enrobée dégradable dotée d'une durée de vie améliorée et son procédé de fabrication. |
WO2002076227A1 (fr) * | 2001-03-23 | 2002-10-03 | Gumlink A/S | Chewing-gum enrobe degradable a duree de vie prolongee et ses procedes de preparation |
US7507427B2 (en) | 2001-03-23 | 2009-03-24 | Gumlink A/S | Coated degradable chewing gum with improved shelf life and process for preparing same |
ES2190875A1 (es) * | 2001-06-12 | 2003-08-16 | Cafosa Gum S A | Goma base degradable y los chicles obtenidos con las mismas. |
EP1994834A1 (fr) * | 2002-09-24 | 2008-11-26 | Gumlink A/S | Gomme à mâcher à faible humidité |
US7833555B2 (en) | 2002-09-24 | 2010-11-16 | Gumlink A/S | Chewing gum comprising at least two different biodegradable polymers |
US8293295B2 (en) | 2002-09-24 | 2012-10-23 | Gumlink A/S | Chewing gum comprising at least two different biodegradable polymers |
US8591967B2 (en) | 2002-09-24 | 2013-11-26 | Gumlink A/S | Biodegradable chewing gum comprising at least one high molecular weight biodegradable polymer |
WO2005063037A1 (fr) * | 2003-12-30 | 2005-07-14 | Gumlink A/S | Gomme a macher comprenant des polymeres biodegradables et ayant une degradabilite acceleree |
WO2010053908A1 (fr) * | 2008-11-06 | 2010-05-14 | Allison Flynn | Bases de gomme à mâcher biodégradables et leurs utilisations |
US9974320B2 (en) | 2011-11-07 | 2018-05-22 | Wm. Wrigley Jr. Company | Chewing gum base containing substituted polysaccharides and chewing gum products made there from |
Also Published As
Publication number | Publication date |
---|---|
EP1246539A4 (fr) | 2004-09-01 |
EP1246539A1 (fr) | 2002-10-09 |
CN1359266A (zh) | 2002-07-17 |
CA2373850A1 (fr) | 2001-01-11 |
AU775784B2 (en) | 2004-08-12 |
AU3916100A (en) | 2001-01-22 |
CA2373850C (fr) | 2005-05-24 |
CN1145421C (zh) | 2004-04-14 |
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