Classifications

• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y301/00—Hydrolases acting on ester bonds (3.1)
  • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
  • C12Y301/01011—Pectinesterase (3.1.1.11)
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L19/00—Products from fruits or vegetables; Preparation or treatment thereof
  • A23L19/09—Mashed or comminuted products, e.g. pulp, purée, sauce, or products made therefrom, e.g. snacks
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
  • A23L2/70—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter
  • A23L2/84—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter using microorganisms or biological material, e.g. enzymes
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L21/00—Marmalades, jams, jellies or the like; Products from apiculture; Preparation or treatment thereof
  • A23L21/10—Marmalades; Jams; Jellies; Other similar fruit or vegetable compositions; Simulated fruit products
  • A23L21/11—Marmalades; Jams; Jellies; Other similar fruit or vegetable compositions; Simulated fruit products obtained by enzymatic digestion of fruit or vegetable compositions
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L23/00—Soups; Sauces; Preparation or treatment thereof
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
  • A23L27/60—Salad dressings; Mayonnaise; Ketchup
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
  • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
  • A23L27/60—Salad dressings; Mayonnaise; Ketchup
  • A23L27/63—Ketchup
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01025—Beta-mannosidase (3.2.1.25), i.e. mannanase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01032—Xylan endo-1,3-beta-xylosidase (3.2.1.32), i.e. endo-1-3-beta-xylanase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01055—Alpha-N-arabinofuranosidase (3.2.1.55)

Definitions

• the present invention relates to a process in which the well known effect of pectinesterase (EC 3.1.1.11, "Enzyme
• a range of extracted plant derived hydrocolloids are traditionally used as texturizing agents for various food products.
• many food products, such as fruits and vegetables in themselves contain hydrocolloids, i.e. the plant cell wall material.
• hydrocolloids i.e. the plant cell wall material.
• the plant cell wall has a very complex nature consisting of different polysaccharides, small amounts of glycoproteins and phenolic compounds.
• the polysaccharides are traditionally divided into cellulose compounds, hemicellulose and pectic compounds.
• the primary cell wall of most flowering plants are of the type I cell wall.
• a type I cell wall the cellulose microfibrils are interlaced with xyloglucan polymers (approx. 50% of the total mass) .
• the cellulose-xyloglucan framework is embedded in a matrix of pectic polysaccharides.
• the pectic matrix consists of smooth regions of polygalacturonic acids and of rhamnogalacturonan.
• the polygalacturonic acid areas are usually highly esterified by methoxyl groups, acetylation of the hydroxy groups also occurs. Side groups consisting of araban, galactan and arabinogalactan are attached to the rhamnogalacturonan residues.
• the pectic polysaccharides constitute approx. 30% of the total mass. Mannans, ⁇ - (1-3) -glucans and arabinoxylans also play a role as pectic-interlocking agents.
• the cell wall further consists of structural proteins, of which extensin is thought to play the major role.
• HM pectin highly methoxylated content of pectin
• LM pectin low methoxylated pectin
• PE pectinesterase
• the present invention relates to a process for the treatment of a pectinaceous homogenate or slurry, wherein said homogenate or slurry is subjected to: a) a treatment with a mixture of enzymes, comprising one or more among galactanases, arabinanases, ⁇ -arabinofura- nosidases, rhamnogalacturonan acetyl esterases (RGAE) , endoglucanases, mannanases, xylanases, and proteolytic enzymes, b) a treatment with a pectinesterase (PE) , which PE is essen ⁇ tially free from pectic depolymerizing enzymes, followed by c) an enzyme inactivating treatment, said process being performed in the presence of divalent metal ions, especially Ca 2+ , said ions being inherently present in said homogenate or slurry, or said ions being added at any time prior to, during or after
• a mixture of enzymes
• the invention furthermore relates to a mixture of enzymes comprising one or more among galactanases, arabinanases, ⁇ - arabinofuranosidases, rhamnogalacturonan acetyl esterases (RGAE), endoglucanases, mannanases, xylanases, and proteolytic enzymes, which mixture is substantially free from pectic depolymerizing enzymes.
• RGAE rhamnogalacturonan acetyl esterases
• endoglucanases mannanases
• xylanases xylanases
• proteolytic enzymes which mixture is substantially free from pectic depolymerizing enzymes.
• the invention in a third aspect relates to the use of such a mixture for the treatment of a pectinaceous homogenate or slurry in combination with a concurrent or sequential treatment with a PE.
• the invention relates to a product produced by the method of the first aspect of the invention.
• the present invention relates to a process for the treatment of a pectinaceous homogenate or slurry, wherein said homogenate or slurry is subjected to: a) a treatment with a mixture of enzymes, comprising one or more among galactanases, arabinanases, ⁇ -arabinofura- nosidases, rhamnogalacturonan acetyl esterases (RGAE), endoglucanases, mannanases, xylanases, and proteolytic enzymes, b) a treatment with a pectinesterase (PE) , which PE is essen ⁇ tially free from pectic depolymerizing enzymes, followed by c) an enzyme inactivating treatment, said process being performed in the presence of divalent metal ions, especially Ca 2+ , said ions being inherently present in said homogenate or slurry, or said ions being added at any time prior to, during or after the process steps (a) to (c)
• Cellulytic and hemicellulytic enzymes such as xylanases, endoglucanases, and mannanases have the ability to loosen the pectic material and presumably to make it more susceptible to the action of specific pectinolytic enzymes.
• Pectinolytic enzymes such as galactanases, arabinanases, ⁇ -arabinofuranosidases, and rhamnogalacturonan acetyl esterases (RGAE) can be used for a sort of debranching of the pectic polysaccharides.
• proteases may as well show an impact on the availability of pectin.
• proteases may be acid proteases, alkaline proteases, highly alkaline proteases and metallo-proteases. More specific definitions of the above enzymes can be found in "Enzyme Nomenclature 1992 " Academic Press, Inc., 1992.
• the debranching of the pectin molecules may also in certain cases introduce a viscosity increase as explained below. It is well known from the literature that the structure of the polymer is of importance in determining the functional properties.
• Linear polysaccharides of the same molecular weight as that of a branched polysaccharide will show higher viscosity, as the linear polymer can gyrate, causing the molecule to sweep through large volumes of space. Therefore the linear molecules will come into contact with each other more easily, and increase the friction or the viscosity characteristics of the solution at much lower concentrations than will highly branched molecules (cf. Glicksman M. , 1982, Food Hydrocolloids 1, 4-10)
• the acetyl groups of the hairy regions may be partially removed by rhamnogalacturonan acetyl esterase. This will improve the hydrophilicity and thus change the resistance to shearing. Glicksman ( supra) discusses these aspects and mentions that the charge of a linear polymer is of importance for its stabilising effect.
• the process may be performed by treating the material with the PE and the mixture of enzymes simultaneously, or, according to further embodiments the treatments may be performed sequentially with the PE treatment either prior to or after the treatment with the enzyme mixture.
• the enzyme inactivation step may be performed after each of the treatments mentioned above.
• the process of the invention may be performed on pectinaceous homogenates or slurries comprising plant parts, and/or material of animal origin.
• the plant parts are normally selected from fruits and vegetables, especially such as apples, tomatoes, oranges, lemons, grapes, lime, pears, berries, such as blackcurrant, strawberries, carrots, and peas.
• the homogenate or slurry will often be selected among juice, puree, concentrate, ketchup, condiment, sauce, soup, salsa, chutney, yoghurt, and deserts.
• treatment (a) is performed at a temperature from 10°C to 60°C, preferably from 30°C to 50°C, a pH from 2 to 7, preferably from 3 to 5, and for a time from 2 to 120 minutes, preferably from 30 to 60 minutes;
• treatment (b) is performed at a temperature from 5°C to 50°C, preferably from 20°C to 40°C, a pH from 2 to 7, preferably from 3 to 5, and for a time from 2 to 120 minutes, preferably from 30 to 60 minutes;
• treatment (c) is a heat inactivation, preferably performed at a temperature from 80°C to 100°C, preferably 85°C and 90°C for a time from 10 seconds to 600 seconds.
• the following conditions may be employed, whereby the process is performed at a temperature from 10°C to 50°C, preferably from 30°C to 40°C, a pH from 2 to 7, preferably from 3 to 5, and for a time from 2 to 120 minutes, preferably from 30 to 60 minutes.
• the enzyme mixture will normally be applied in an amount from 5 to 150, preferably from 7 to 100, and better from 10 to 50 mg enzyme protein per kg homogenate or slurry for each of the enzymes.
• the amount in FXU (Farvet Xylan Unit) will be from 150 to 4000, preferably from 225 to 3000, and better from 300 to 1500 FXU per kg homogenate or slurry.
• the PE will normally be applied in an amount from 2 to 60, preferably from 5 to 40, and better from 10 to 25 PEU per kg homogenate or slurry.
• PEU Pectin Esterase Units
• the mixture of enzymes and the PE is applied in a ratio from 1:10 to 50:1, preferably from 1:2 to 5:1, whereby the amounts of both componen ⁇ ts are on a weight of protein measure.
• the invention further relates to a mixture of enzymes comprising one or more among galactanases, arabinanases, ⁇ - arabinofuranosidases, rhamnogalacturonan acetyl esterases (RGAE) , endoglucanases, mannanases, xylanases, and proteolytic enzymes, especially proteases.
• RGAE rhamnogalacturonan acetyl esterases
• the PE used in the invention is derived from a fungus of the genus Aspergillus, preferably A . japonicus , (S. Ishii et al . , 1979, Journal of Food Science 44, p 611-614), A . aculea tus , A . niger (EP 0 388 593 Al) , A . awa ori (EP 0 388 593 Al) , or the genera Fusarium, Sclerotonia , or PenicilliuiT., (Kikkoman: DE 2843351; US 4,200,694) . These pectinesterases exhibit a relatively low pH optimum, corresponding to the relatively low pH optimum of many fruits.
• the pectinesterase is an enzyme preparation substantially free from pectin depolymerizing enzymes.
• Such enzymes are obtainable by using a host system for the expression of the enzyme which does not produce any pectin depolymerizing enzymes (WO 94/25575) .
• the invention also relates to the use of a mixture as defined above for the treatment of a pectinaceous homogenate or slurry.
• the invention relates to a gel produced by the method of the invention.
• Such a gel may be a jam, marmalade, jelly, juice, paste, soup, dressing, sauce,, condiment, ketchup, salsa, chutney, pudding, mousse, or other desert.
• Enzymes PE, RGAE, galactanase, arabinanase, ⁇ -arabinofuranosi- dase, endo glucanase III, protease II.
• the production of these enzymes are indicated in: (galactanase) WO 92/13945, (arabinases)
• the xylanolytic activity can be expressed in FXU-units, determined at pH 6.0 with remazol-xylan (4-O-methyl-D-glucurono- D-xylan dyed with Remazol Brilliant Blue R, Fluka) as substrate.
• a xylanase sample is incubated with the remazol-xylan substrate.
• the background of non-degraded dyed substrate is precipitated by ethanol .
• the remaining blue colour in the supernatant is proportional to the xylanase activity, and the xylanase units are then determined relatively to an enzyme standard at standard reaction conditions, i.e. at 50.0 °C, pH 6.0, and 30 minutes reaction time.
• SMS Texture Analyser TA-XT2 (Stable Micro Systems, XT.RA Dimen ⁇ sions, Operating Manual version 37)
• the gel strength/hardness of the slurries was measured by the Texture Analyzer by compression analysis.
• the compression was carried out by using a flat cylinder, f 20 mm and with a speed of 2.0 mm/s. The compression make up a total of 20 % of the sample height. From the record of the force-time curve the gel strength measured as the peak force, is directly obtained. The gel strength was measured as an average of four measurements and is given in N.
• Viscosity Measurements The viscosity was measured by Spindel C, specification no. 93. Measurements at shear rate 2.5 rpm and 20 rpm were carried out.
• Sample No. 2 PE 10.5 PEU/kg slurry
• Sample No. 3 RGAE, galactanase, arabinanase, ⁇ -arabinofura- nosidase, endo glucanase III, protease II, 25 mg/kg slurry of each of the enzymes.
• EXAMPLE 2 Fresh broccoli was washed and chopped into smaller pieces. Water was added 1:1 and then the vegetables was cooked for 15 min. The mixture was then chopped in a meat mincer (2 mm holes) . Four samples of 200 g were adjusted to 40°C and added enzymes as follows :
• Sample No. 2 PE 10.5 PEU/kg slurry
• Sample No. 3 RGAE, galactanase, arabinanase, ⁇ -arabinofura- nosidase, endo glucanase III, protease II, 25 mg/kg slurry of each of the enzymes.
• Hot break tomato paste was diluted from 23% soluble solids to 8.5% soluble solids and homogenised in a homogeniser at 300 bar. Afterwards samples of 455 g were weighed out in 1000 ml containers, the temperature was adjusted to 40 °C.
• Enzyme preparation Ten portions of 455 g substrate were prepared and added enzyme as follows:
• PE 10.5 PEU/kg undiluted paste + Xylanase II, 810 FXU/kg undiluted paste
• PE 10.5 PEU/kg undiluted paste + Xylanase I , 810 FXU/kg undiluted paste
• the samples were incubated for 30 min at 40°C.
• ketchup was prepared by adding 300 g of brine.
• the brine consist of sugar, salt and acetic acid (Skott, W. P. Die Industrielle Obst - und Gemuseverêt, 1970 55 229-234) .
• the prepared ketchups were then heat treated, 88°C in 3 min.
• the ketchup samples were then distributed and cooled in an ice bath and finally placed in the refrigerator until analysis could take place. The results appears from Table III.
• Viscosity Viscosity 2.5 rpm 20 rpm cP cP

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• Jellies, Jams, And Syrups (AREA)
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• 1996
  • 1996-09-16 ZA ZA967790A patent/ZA967790B/xx unknown
  • 1996-09-17 IL IL12342596A patent/IL123425A0/xx unknown
  • 1996-09-17 JP JP9512330A patent/JPH11511330A/ja active Pending
  • 1996-09-17 EP EP96930032A patent/EP0851736A1/en not_active Withdrawn
  • 1996-09-17 AU AU69238/96A patent/AU710702B2/en not_active Ceased
  • 1996-09-17 NZ NZ316894A patent/NZ316894A/xx unknown
  • 1996-09-17 WO PCT/DK1996/000391 patent/WO1997010726A1/en not_active Application Discontinuation
  • 1996-09-18 AR ARP960104400A patent/AR003616A1/es unknown
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