WO1997003574A1 - Process for stabilizing proteins in an acidic environment with a high-ester pectin - Google Patents
Process for stabilizing proteins in an acidic environment with a high-ester pectin Download PDFInfo
- Publication number
- WO1997003574A1 WO1997003574A1 PCT/EP1996/003051 EP9603051W WO9703574A1 WO 1997003574 A1 WO1997003574 A1 WO 1997003574A1 EP 9603051 W EP9603051 W EP 9603051W WO 9703574 A1 WO9703574 A1 WO 9703574A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- pectin
- recombinant
- pme
- enzyme
- nucleotide sequence
- Prior art date
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- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 229910000027 potassium carbonate Inorganic materials 0.000 description 1
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
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- 229910052939 potassium sulfate Inorganic materials 0.000 description 1
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- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
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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
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C21/00—Whey; Whey preparations
- A23C21/08—Whey; Whey preparations containing other organic additives, e.g. vegetable or animal products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/13—Fermented milk preparations; Treatment using microorganisms or enzymes using additives
- A23C9/137—Thickening substances
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/152—Milk preparations; Milk powder or milk powder preparations containing additives
- A23C9/154—Milk preparations; Milk powder or milk powder preparations containing additives containing thickening substances, eggs or cereal preparations; Milk gels
- A23C9/1542—Acidified milk products containing thickening agents or acidified milk gels, e.g. acidified by fruit juices
-
- 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
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
- A23L29/206—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of vegetable origin
- A23L29/231—Pectin; Derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
Abstract
Description
Claims
Priority Applications (11)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE69615199T DE69615199T3 (en) | 1995-07-14 | 1996-07-12 | PROCESS FOR THE STABILIZATION OF PROTEINS IN ACID SURFACES USING HIGHLY VERTESTED PECTINS |
AT96925730T ATE205366T1 (en) | 1995-07-14 | 1996-07-12 | METHOD FOR STABILIZING PROTEINS IN ACIDIC ENVIRONMENTS USING HIGHLY ESTERIFIED PECTINS |
BR9609791A BR9609791A (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic medium with a high ester pectin |
NZ313625A NZ313625A (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
PL96324503A PL185172B1 (en) | 1995-07-14 | 1996-07-12 | Method of stabilising proteins in an acid environment by means of high-ester pectin |
EP96925730A EP0839006B2 (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
AU66144/96A AU714570B2 (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
JP9506259A JPH11509102A (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins using high ester pectin in acidic environment |
MX9800422A MX9800422A (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic environment with a high-ester pectin. |
DK96925730.2T DK0839006T4 (en) | 1995-07-14 | 1996-07-12 | Method for Stabilizing Proteins in an Acidic Environment with a High Ester Pectin |
US10/165,528 US7166312B2 (en) | 1995-07-14 | 2002-06-07 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GBGB9514438.2A GB9514438D0 (en) | 1995-07-14 | 1995-07-14 | Stabilisation process and an enzyme for use in such a process |
GB9514438.2 | 1995-07-14 |
Related Child Applications (3)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US08983364 A-371-Of-International | 1998-05-18 | ||
US09/413,068 Division US6268195B1 (en) | 1995-07-14 | 1999-10-06 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
US10/165,528 Division US7166312B2 (en) | 1995-07-14 | 2002-06-07 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
Publications (1)
Publication Number | Publication Date |
---|---|
WO1997003574A1 true WO1997003574A1 (en) | 1997-02-06 |
Family
ID=10777675
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/EP1996/003051 WO1997003574A1 (en) | 1995-07-14 | 1996-07-12 | Process for stabilizing proteins in an acidic environment with a high-ester pectin |
Country Status (20)
Country | Link |
---|---|
US (4) | US6268195B1 (en) |
EP (5) | EP0976822A3 (en) |
JP (3) | JPH11509102A (en) |
CN (1) | CN1112855C (en) |
AT (2) | ATE205366T1 (en) |
AU (1) | AU714570B2 (en) |
BR (1) | BR9609791A (en) |
CA (1) | CA2225481A1 (en) |
CZ (1) | CZ11798A3 (en) |
DE (2) | DE69635625T2 (en) |
DK (2) | DK0839006T4 (en) |
ES (2) | ES2253179T3 (en) |
GB (1) | GB9514438D0 (en) |
HK (1) | HK1035846A1 (en) |
MX (1) | MX9800422A (en) |
NZ (1) | NZ313625A (en) |
PL (1) | PL185172B1 (en) |
PT (1) | PT839006E (en) |
RU (1) | RU2207761C2 (en) |
WO (1) | WO1997003574A1 (en) |
Cited By (19)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2778667A1 (en) * | 1998-05-12 | 1999-11-19 | Danisco | Amino acid sequence useful for producing modified pectin methyl esterase enzymes for preparing deesterified pectin for use in foods |
WO2000008952A1 (en) * | 1998-08-14 | 2000-02-24 | Danisco A/S | Use of a composition |
GB2342921A (en) * | 1998-10-24 | 2000-04-26 | Zylepsis Ltd | Demethoxylation of pectins, plant extracts containing PME and the uses thereof |
WO2000027888A1 (en) * | 1998-11-05 | 2000-05-18 | Cp Kelco Aps | Pectin for stabilizing proteins |
FR2789267A1 (en) * | 1999-02-08 | 2000-08-11 | Gervais Danone Co | CARBONATE AND LACTIZED BEVERAGE AND PROCESS FOR PREPARING SAME |
WO2000058367A1 (en) * | 1999-03-31 | 2000-10-05 | Hercules Incorporated | Pectin having reduced calcium sensitivity |
WO2000078982A1 (en) * | 1999-06-17 | 2000-12-28 | Danisco A/S | Process for the enzymatic modification of pectin |
US6274548B1 (en) * | 1998-05-13 | 2001-08-14 | Carrington Laboratories, Inc. | Pectic substance as a growth factor stabilizer |
US6368642B2 (en) | 1997-04-24 | 2002-04-09 | Danisco A/S | Composition comprising pectin methyl esterase and two substrates |
US6428837B1 (en) | 2000-06-09 | 2002-08-06 | Cp Kelco Aps | Deesterified pectins, processes for producing such pectins, and stabilized acidic liquid systems comprising the same |
JP2002330710A (en) * | 2001-02-20 | 2002-11-19 | Fuji Oil Co Ltd | Method for producing dispersion stabilizer and dispersion-stabilized product |
US6627429B1 (en) * | 1998-09-16 | 2003-09-30 | Danisco A/S | Process for enzymatically modifying pectin |
US6699977B1 (en) | 2000-06-09 | 2004-03-02 | Cp Kelco Aps | Low methoxyl pectins, processes thereof, and stabilized aqueous systems comprising the same |
US6890578B1 (en) * | 1999-08-27 | 2005-05-10 | Fuji Oil Co., Ltd. | Acidic protein foods, process for their production and stabilizer |
US7053268B1 (en) | 1999-06-17 | 2006-05-30 | Danisco A/S | Promoter |
GB2482108A (en) * | 2010-06-09 | 2012-01-25 | Milk & Fruit Company Ltd | Beverage having milk and fruit constituents |
US8211484B2 (en) | 2003-08-19 | 2012-07-03 | Dupont Nutrition Biosciences Aps | Process for preparing a food product using depolymerised pectin as stabiliser |
EP2888946A1 (en) * | 2013-12-24 | 2015-07-01 | DMK Deutsches Milchkontor GmbH | Use of pektin for improving the sensorial properties of compositions based on acidic whey |
US10660345B2 (en) | 2012-07-13 | 2020-05-26 | Kabushiki Kaisha Yakult Honsha | Pectin-containing acidic milk beverage and production method thereof |
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GB9514438D0 (en) * | 1995-07-14 | 1995-09-13 | Danisco | Stabilisation process and an enzyme for use in such a process |
US7022683B1 (en) | 1998-05-13 | 2006-04-04 | Carrington Laboratories, Inc. | Pharmacological compositions comprising pectins having high molecular weights and low degrees of methoxylation |
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US6777000B2 (en) * | 2001-02-28 | 2004-08-17 | Carrington Laboratories, Inc. | In-situ gel formation of pectin |
SE0103613D0 (en) * | 2001-10-30 | 2001-10-30 | Astrazeneca Ab | Novel formulation |
US6887508B2 (en) * | 2002-02-20 | 2005-05-03 | Solae, Llc | Protein stabilizing agent |
NZ535989A (en) * | 2002-05-16 | 2006-05-26 | Firmenich & Cie | Flavoured oil-in-water emulsions for food applications |
US20040022876A1 (en) * | 2002-07-30 | 2004-02-05 | Nancy Green | Cardiovascular health enhancement with soy fortified citrus juice compositions |
US20040022877A1 (en) * | 2002-07-30 | 2004-02-05 | Nancy Green | Cardiovascular health enhancement with soy fortified orange juice compositions |
US7229659B2 (en) * | 2003-06-17 | 2007-06-12 | Solae, Llc | Process for making stable protein based acid beverage |
US7510737B2 (en) * | 2003-10-24 | 2009-03-31 | Unilever Bestfoods, North America, Division Of Conopco, Inc. | Low carbohydrate fiber containing emulsion |
US20050123649A1 (en) * | 2003-11-05 | 2005-06-09 | Kerry Group Services International, Ltd. | Acid-stable soy protein and fortified food or beverage |
US7038274B2 (en) | 2003-11-13 | 2006-05-02 | Volterra Semiconductor Corporation | Switching regulator with high-side p-type device |
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Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1994025575A1 (en) * | 1993-04-30 | 1994-11-10 | Novo Nordisk A/S | An enzyme exhibiting pectin methylesterase activity |
EP0709033A1 (en) * | 1994-10-17 | 1996-05-01 | Kabushiki Kaisha Yakult Honsha | Method for producing calcium enriched fermented milk and fermented milk drink and the products |
JPH08112059A (en) * | 1994-10-17 | 1996-05-07 | Yakult Honsha Co Ltd | Production of calcium-enriched lactic acid beverage and product thereof |
Family Cites Families (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CH474218A (en) | 1967-03-17 | 1969-06-30 | Nestle Sa | Method and apparatus for separating proteins from a protein solution or suspension |
US4200694A (en) * | 1977-10-08 | 1980-04-29 | Kikkoman Shoyu Co., Ltd. | Novel pectin esterase, process for its production, and process for producing demethoxylated pectin by the use of said pectin esterase |
US4391830A (en) * | 1981-05-21 | 1983-07-05 | Coca Cola Company | Production of liquid yogurt stabilized with high methoxyl pectin |
US4462932A (en) | 1983-06-22 | 1984-07-31 | Purdue Research Foundation | Isolation of native casein by cryodestabilization |
GB9127098D0 (en) | 1991-12-20 | 1992-02-19 | Ici Plc | Dna,dna constructs,cells and plants derived therefrom |
DE69313102T2 (en) * | 1993-06-11 | 1997-12-11 | Nestle Sa | Composition for heat stabilization of proteins and product therefrom |
US6143346A (en) * | 1993-12-02 | 2000-11-07 | Hercules Incorporated | Pectin process and composition |
JP2800103B2 (en) * | 1995-04-17 | 1998-09-21 | 日精樹脂工業株式会社 | Runnerless mold |
GB9514438D0 (en) * | 1995-07-14 | 1995-09-13 | Danisco | Stabilisation process and an enzyme for use in such a process |
US6221419B1 (en) * | 1998-11-05 | 2001-04-24 | Hercules Incorporated | Pectin for stabilizing proteins |
-
1995
- 1995-07-14 GB GBGB9514438.2A patent/GB9514438D0/en active Pending
-
1996
- 1996-07-12 JP JP9506259A patent/JPH11509102A/en not_active Withdrawn
- 1996-07-12 CA CA002225481A patent/CA2225481A1/en not_active Abandoned
- 1996-07-12 ES ES00204485T patent/ES2253179T3/en not_active Expired - Lifetime
- 1996-07-12 EP EP99201871A patent/EP0976822A3/en not_active Withdrawn
- 1996-07-12 BR BR9609791A patent/BR9609791A/en not_active Application Discontinuation
- 1996-07-12 AU AU66144/96A patent/AU714570B2/en not_active Ceased
- 1996-07-12 EP EP00204485A patent/EP1101412B1/en not_active Revoked
- 1996-07-12 AT AT96925730T patent/ATE205366T1/en active
- 1996-07-12 MX MX9800422A patent/MX9800422A/en unknown
- 1996-07-12 WO PCT/EP1996/003051 patent/WO1997003574A1/en not_active Application Discontinuation
- 1996-07-12 CZ CZ98117A patent/CZ11798A3/en unknown
- 1996-07-12 EP EP05021763A patent/EP1621082A3/en not_active Withdrawn
- 1996-07-12 PT PT96925730T patent/PT839006E/en unknown
- 1996-07-12 CN CN96196968A patent/CN1112855C/en not_active Expired - Lifetime
- 1996-07-12 AT AT00204485T patent/ATE313270T1/en not_active IP Right Cessation
- 1996-07-12 EP EP96925730A patent/EP0839006B2/en not_active Expired - Lifetime
- 1996-07-12 PL PL96324503A patent/PL185172B1/en not_active IP Right Cessation
- 1996-07-12 RU RU98102779/13A patent/RU2207761C2/en not_active IP Right Cessation
- 1996-07-12 DE DE69635625T patent/DE69635625T2/en not_active Revoked
- 1996-07-12 NZ NZ313625A patent/NZ313625A/en unknown
- 1996-07-12 EP EP05022863A patent/EP1625796A1/en not_active Withdrawn
- 1996-07-12 DK DK96925730.2T patent/DK0839006T4/en active
- 1996-07-12 DE DE69615199T patent/DE69615199T3/en not_active Expired - Lifetime
- 1996-07-12 DK DK00204485T patent/DK1101412T3/en active
- 1996-07-12 ES ES96925730T patent/ES2163644T5/en not_active Expired - Lifetime
-
1999
- 1999-10-06 US US09/413,068 patent/US6268195B1/en not_active Expired - Lifetime
- 1999-10-06 US US09/413,452 patent/US6083540A/en not_active Expired - Lifetime
-
2001
- 2001-03-16 US US09/770,940 patent/US20020009790A1/en not_active Abandoned
- 2001-09-17 HK HK01106553A patent/HK1035846A1/en not_active IP Right Cessation
-
2002
- 2002-06-07 US US10/165,528 patent/US7166312B2/en not_active Expired - Fee Related
-
2004
- 2004-12-22 JP JP2004371762A patent/JP2005124579A/en active Pending
-
2006
- 2006-04-28 JP JP2006127112A patent/JP2006262905A/en active Pending
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1994025575A1 (en) * | 1993-04-30 | 1994-11-10 | Novo Nordisk A/S | An enzyme exhibiting pectin methylesterase activity |
EP0709033A1 (en) * | 1994-10-17 | 1996-05-01 | Kabushiki Kaisha Yakult Honsha | Method for producing calcium enriched fermented milk and fermented milk drink and the products |
JPH08112059A (en) * | 1994-10-17 | 1996-05-07 | Yakult Honsha Co Ltd | Production of calcium-enriched lactic acid beverage and product thereof |
Non-Patent Citations (6)
Title |
---|
"Food Ingredients Europe - Conference Proceedings", 1994, PPE, MAARSEN - THE NETHERLANDS, XP002016403 * |
A.C.M. VAN HOOYDONK: "De Bereiding van Drinkyoghurt: 2. De Invloed van de Produktsamenstelling", VOEDINGSMIDDELEN TECHNOLOGIE, vol. 15, no. 20, 1982, ZEIST NL, pages 25 - 29, XP002016401 * |
DATABASE WPI Section Ch Week 9628, Derwent World Patents Index; Class D13, AN 96-271372, XP002016404 * |
FEBS LETTERS, vol. 355, 1994, AMSTERDAM NL, pages 135 - 139, XP002021517 * |
PLANT MOLECULAR BIOLOGY, vol. 25, DORDRECHT NL, pages 313 - 318, XP002021518 * |
R. KOHN: "Die Verteilung der Freien und Veresterten Carboxylgruppen im Pektinmolekül nach Einwirkung von Pektinesterase aus A.Niger und Orangen", DIE NAHRUNG, vol. 19, no. 1, 1985, pages 75 - 85, XP002016402 * |
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