WO2012146717A1 - Préparation d'une composition de blanc d'œuf - Google Patents

Préparation d'une composition de blanc d'œuf Download PDF

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Publication number
WO2012146717A1
WO2012146717A1 PCT/EP2012/057767 EP2012057767W WO2012146717A1 WO 2012146717 A1 WO2012146717 A1 WO 2012146717A1 EP 2012057767 W EP2012057767 W EP 2012057767W WO 2012146717 A1 WO2012146717 A1 WO 2012146717A1
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WIPO (PCT)
Prior art keywords
egg white
protease
process according
composition
white composition
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Ceased
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PCT/EP2012/057767
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English (en)
Inventor
Henriëtte Maria Wilhelmina Jacoba Catharina UIJEN
Cecile Veerman
Arjen Sein
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DSM IP Assets BV
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DSM IP Assets BV
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Classifications

    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L15/00—Egg products; Preparation or treatment thereof
    • A23L15/25—Addition or treatment with microorganisms or enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A23L29/275—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of animal origin, e.g. chitin

Definitions

  • the present invention relates to a process for the preparation of an egg white composition.
  • Egg white is a desirable ingredient for many foods such as bakery products, meringues and meat products because of its excellent foaming and gelling properties (J. Food Engineering 83 (2007) 404-413).
  • Egg white consists mainly of protein (10 % w/w) and 0.5-0.6 % w/w carbohydrates, mainly glucose.
  • the protein part of egg white can be devided into several classes of proteins, such as ovalbumin, ovotransferrin, ovomucoid, ovomucin and lysozyme (Y. Mine, Trends in Food Sci Techn. 1995, vol 6, p 225-232).
  • egg white is usually de-sugared and spray-dried followed by a so called hot room treatment of about 4 weeks at about 70-85 degrees Celsius in order to reduce microbial contamination and restore functional property losses due to spray drying.
  • a disadvantage of heating spray-dried egg white is that it is a very time and energy consuming process. The process from egg breaking to sales of spray dried egg white takes about 6 weeks.
  • the aim of the present invention is an improved process for the preparation of egg white with good gelling and/or foaming properties, which is less time and energy consuming than known in the art.
  • the present invention relates to a process for preparing an egg white composition, comprising incubating egg white with a protease such that an egg white composition is prepared that has an increased gelling temperature compared to egg white that has not been treated with a protease.
  • the invention further relates to an egg white composition obtainable by a process according to the present disclosure.
  • an advantage of an egg white composition according to the present invention is that the egg white composition formed a gel at a higher temperature than untreated egg white and that it was able to pasteurize the egg white composition without loosing foaming and gelling properties. It was found that the egg white composition as disclosed herein had a gelling temperature that is 1 to 15 degrees Celsius higher, for example 2 to 14, or 3 to 12 degrees Celsius higher, than egg white that has not been incubated with a protease.
  • the present disclosure relates to a process for preparing an egg white composition, comprising incubating egg white with a protease such that an egg white composition is prepared that has an increased gelling temperature compared to egg white that has not been treated with a protease.
  • Gelling temperature of an egg white is defined herein as the temperature at which an egg white (composition) starts to form a gel, upon heating of the egg white (composition).
  • the wording gelling and gelation have the same meaning and are used interchangeably.
  • temperature or gel point can be measured by rheometry, in an experiment where the temperature of egg white is slowly increased while the elastic modulus (G') and the loss or viscosity modulus (G") are measured.
  • Egg white as used in the present disclosure is used to indicate the clear liquid contained within an egg.
  • Egg white is usually obtained by separating fresh eggs in egg yolk and egg white.
  • Egg white in the process according to the present invention may be any suitable egg white.
  • Egg white may be homogenized before it is used in a process according to the present invention.
  • Egg white may be homogenized by incubating egg white at a temperature of 0- 10 degrees Celsius, for instance 1 to 8 degrees Celsius at a pH value of the egg white (pH 8.5-9.5). Said incubation step is usually followed by a step of centrifuging the egg white. The supernatant obtained by centrifuging egg white is egg white that is homogenized. Centrifuging egg white may be carried out by any suitable method known by the skilled person in the art.
  • Egg white may be incubated with any suitable protease in a process according to the present invention which, results in an increased gelling temperature of an egg white composition.
  • a protease is defined herein as an enzyme that hydrolyses the peptide bonds that link amino acids in a polypeptide chain that form a protein.
  • proteases The internationally recognized schemes for the classification and nomenclature of all enzymes from IUMB include proteases.
  • the updated IUMB text for protease EC numbers can be found at the internet site: http://www.chem.qmw/ac.uk/iubmb/enzyme/EC3/4/1 1/.
  • enzymes are defined by the fact that they catalyze a single reaction. This has the important implication that several different proteins are all described as the same enzyme, and a protein that catalyses more than one reaction is treated as more than one enzyme.
  • Endoproteases are those enzymes that hydrolyze internal peptide bonds of proteins and exoproteases are those enzymes that hydrolyze peptide bonds adjacent to a terminal oarmino group (so-called “aminopeptidases”), or a peptide bond between the terminal carboxyl group and the penultimate amino acid (so-called “carboxypeptidases”).
  • aminopeptidases enzymes that hydrolyze peptide bonds adjacent to a terminal oarmino group
  • carboxyl group a terminal carboxyl group and the penultimate amino acid
  • serine endoproteases EC 3.4.21
  • cysteine endoproteases EC 3.4.22
  • aspartic endoproteases EC 3.4.23
  • metalloendoproteases EC 3.4.24
  • threonine endoproteases EC 3.4.25
  • a suitable protease in a process according to the present disclosure may for instance belong to a group selected from aspartic endoproteases, metalloendoproteases, and serine endoprotease.
  • Suitable aspartic endoproteases may for instance be aspergillopepsin I (EC 3.4.23.18) or aspergillopepsin II (EC 3.4.23.19).
  • Suitable metalloendoproteases may for instance be bacillolysin (EC. 3.4.24.28).
  • a suitable serine endoprotease may for instance be subtilisin (EC 3.4.21 .62) Aspegillopepsin I and II are usually produced by a fungus belonging to the genus Aspergillus, for instance an A. niger. Bacillolysin and subtilisin may be produced by Bacillus sp.
  • a protease in a process according to the present disclosure may comprise one or more proteases.
  • a protease may comprise a mixture of aspergillopepsin I and aspergillopepsin II, or any other suitable mixtures of proteases.
  • a process as described herein comprises incubating egg white with a protease such that an egg white composition is prepared comprising a degree of hydrolysis of between 0.1 and 30%, for instance between 0.5 and 20%, for instance between 1 and 10%.
  • a method to determine the degree of hydrolysis is by using orthophtalic anhydride (OPA), which reacts with any terminal aminogroup, such as described in Nielsen et. al. (2001 ) J. Food Science Vol.66, No. 5, p. 642-646.
  • OPA orthophtalic anhydride
  • the amount of reacted OPA can be quantified using UVA IS spectrometry.
  • the degree of hydrolysis can be expressed as the value of hydrolysed protein versus intact protein.
  • Incubating egg white with a protease such that an egg white composition is prepared that has a higher gelling temperature than egg white may be performed in any suitable way.
  • incubating egg white with a protease as disclosed herein may take place during desugaring of egg white.
  • sugars may cause browning by maillardation.
  • Desugaring the egg white may prevent such browning to occur.
  • Desugaring may be performed by incubating egg white with a glucose oxidase and a catalase or by incubating with yeast, which is known to a skilled person in the art (see for instance V. Lechevalier et. AL, J. Food Eng. 2007, 83, p. 404- 413).
  • Incubating egg white with a protease may be carried out at a pH which is not the optimum pH of a protease, for instance a pH of between 5 and 8.
  • a pH which is not the optimum pH of a protease, for instance a pH of between 5 and 8.
  • the pH is higher or lower than the isoelectric point of egg white proteins.
  • Suitable temperatures at which a egg white may be incubated with a protease in a process according to the present disclosure may be between 4 and 60 degrees Celsius, for instance between 10 and 55 degrees Celsius, for instance between 15 and 52 degrees Celsius.
  • a process as described herein comprises pasteurizing the egg white composition and obtaining a pasteurized egg white composition.
  • An advantage of pasteurizing a liquid egg white composition is that it reduces microbial contamination and may make the time and energy consuming hot room treatment redundant, or can lower the temperature and/or time needed for a hot room treatment. Consequently, the time from breaking eggs to selling eggs can be shortened with weeks when using the process for preparing an egg white composition according to the present disclosure compared to a process for preparing egg white wherein a hot room treatment is applied.
  • Another advantage of pasteurizing an egg white composition in the process according to the present invention is that a microbial safe fluid egg white product can be prepared.
  • Pasteurization of an egg white composition may be carried out in any suitable way.
  • Pasteurization may for instance comprise bringing the egg white composition to a temperature of between 60 to 75 degrees Celsius or 62 to 70 degrees Celsius, for instance for 10 sec to 10 min, for instance for 20 sec to 8 min, for instance for 1 min to 6 min.
  • a process according to the present disclosure comprises a step of spray drying the egg white composition and obtaining a spray-dried egg white composition.
  • Spray drying is a known technology to the skilled person in the art. Spray drying of egg white may be carried out after the egg white is incubated with a protease and heat pasteurized.
  • a process according to the present disclosure further comprises using the egg white composition in the preparation of a food product.
  • Use of an egg white composition according the present disclosure was found particularly suitable in the preparation of a food product that does not undergo a pasteurization step after the egg white has been added to the food product.
  • a suitable food product may for instance be surimi, puddings, pastry, cookies, meringues, cake, glazing on pastry and biscuits, as a binding agent in the meat industry, meat analogues, nougats, batter.
  • an egg white composition obtainable by a process as disclosed herein. It was surprisingly found that an egg white composition according to the present invention results in an increased gelling temperature, such as 1 to 15 degrees Celsius higher, for example 2 to 14, or 3 to 12 degrees Celsius higher, compared to egg white that has not been incubated with a protease.
  • the present disclosure further relates to the use of a protease to increase the gelling temperature of an egg white composition.
  • a protease used to increase the gelling temperature of an egg white composition may be any suitable protease as defined herein above.
  • the increase in gelling temperature may be 1 to 15 degrees Celsius, for example 2 to 14, or 3 to 12 degrees Celsius.
  • the present invention relates to a process for preparing an egg white composition, wherein a protease is used to increase the gelling temperature of egg white and wherein the egg white composition with an increased gelling temperature is produced.
  • the present invention relates to a food product comprising egg white obtainable by a process according to the present invention.
  • a suitable food product may be surimi, bavarois, pudding, pastry, cookies, meringues, cake, glazing on pastry and biscuits, as a binding agent in the meat industry, meat analogues, nougats, batter.
  • the egg white was collected in a small buffer tank, from where it was pumped to the fermentation vessel. After that an intermediate buffering step took place at 0-4 degrees Celsius at given pH of the egg white (pH 8.5-9.5). The time period of this buffering step depends on when the egg white is needed fro further processing, usually between 1 to 96h. Subsequently, the egg white was pumped through a Westfalia plate centrifuge with 4700 rpm, 8000 liters/h for approximately 1 1 seconds centrifuge residence time to a fermentation tank. The supernatant obtained after this centrifuge step was the egg white used in these examples.
  • Aspergillopepsin I protein sequence SEQ ID NO: 128 of WO02/068623
  • Aspergillopepsin II protein sequence SEQ ID NO: 131 of WO 02/068623
  • recovery of the crude enzyme is relatively simple: after fermentation the broth was filtered, the filtrate was sterile filtered and then concentrated on a Pellicon XL Casette Biomax 10 ("Millipore").
  • the subsequent chromatographic purification was carried out by an initial chromatography over a Q- sepharose XK 16/20 column at pH 5.6 followed by a CAIEX chromatography over a SP- Sepharose XK 16/20 column at a pH of 4.2. In both cases the enzyme was eluted using a gradient towards 1 mol/l NaCI. Fractions were collected based on the occurrence of bands of a specific molecular weight detected upon SDS-PAGE followed by Coomassie blue staining.
  • hemoglobin substrate (20g/L, Sigma Aldrich catalogue number H2625) was incubated with aspergillopepsin II enzyme solution at 40 degrees Celsius and a pH of 1 .75.
  • the reaction was terminated by adding trichloric acetic acid (Sigma-Aldrich 27242).
  • the optical density of the supernatant after centrifugation was measured at a wavelength of 275 nm (by UV-VIS Spectrophotometer Hitachi U2910) and was compared to an L-tyrosine solution (Merck, 1 .08371 ) of known strength. The obtained value is a measure for the activity.
  • the activity is expressed in units per gram.
  • One unit is the amount of enzyme that hydrolyses an amount of substrate per minute, under the conditions of the test giving a solution with an optical density at 275 nm equal to the optical density of a solution containing 1 .10 ⁇ g tyrosine per mL in HCI solution of 0.006 mol/L.
  • Egg white was manually separated from fresh eggs, mixed with a Silversion mixer for 10 minutes at 3500 rpm before centrifugation for 10 min at 5.000 rpm to remove debris and chelaza from the native egg white.
  • the pH of the egg white was adjusted to pH 5.6, using 0.5 M citric acid.
  • the egg white was put in a water bath at 50 degrees Celsius for 20 min.
  • One part of this sample was used as a reference sample.
  • the pH of this sample was adjusted to 7.0 using 0.2M NaOH.
  • the other part is incubated with 0.002% (w/v) (2.1 * 10E5 rfu/mg.min) Aspergillopepsin II, prepared as described above at 50 degrees Celsius for 5 hrs. After incubation the pH was adjusted to 7.0 with the use of 0.2 M NaOH. After incubation, the degree of hydrolysis was 1 .70%.
  • the pH of the egg white was adjusted to pH 5.6, using 0.5 M citric acid.
  • the egg white was put in a water bath at 50 degrees Celsius for 20 min.
  • One part of this sample was used as a reference sample.
  • the pH of this sample was adjusted to 7.0 using 0.2M NaOH.
  • the other part is incubated with 0.002% (w/v) (7.6 * 10E5 rfu/mg. min) Aspergillopepsin I prepared as described above at 50 degrees Celsius for 5 hrs. After incubation the pH was adjusted to 7.0 with the use of 0.2 M NaOH and the degree of hydrolysis was 2.00%.
  • the pH of the egg white was adjusted to pH 7, using 0.5 M citric acid.
  • the egg white was put in a water bath at 40 degrees Celsius for 10 min.
  • One part of this sample was used as a reference sample.
  • the other part is incubated with 0.1 % (w/w) Validase BNP-L (DSM, Lotnr. OH0091 H; activity: 2000 NPU/g) at 40 degrees Celsius for 2 hrs. After incubation the pH was adjusted to 7.0 with the use of 0.2 M NaOH. After incubation the degree of hydrolysis was 7.29%.
  • Example 4 Treatment of egg white with Alcalase EC 3.4.21.62
  • the pH of the egg white was adjusted to pH 7, using 0.5 M citric acid.
  • the egg white was put in a water bath at 40 degrees Celsius for 10 min.
  • One part of this sample was used as a reference sample.
  • the other part is incubated with 0.1 % (w/w) Alcalase AF 2.4L Novozymes (Lotnr. RM09481 1 U-09124) at 40 degrees Celsius for 2 hrs. After incubation the pH was adjusted to 7.0 with the use of 0.2 M NaOH.
  • Alcalase 7 The results in Examples 1 to 5 show that incubation of egg white with different proteases increased the gelling temperature of the egg white composition.
  • the foaming properties of the protease treated egg white were as good as untreated egg white or were improved.
  • the gel strength of egg white treated with aspergillopepsin was similar to untreated egg white; the gel strength of egg white treated with metalloendoprotease and serine endoprotease was lower than untreated egg white.
  • Example 6 Treatment of egg white with different doses of Aspergillopepsin II (EC 3.4.23.19) during desugaring of egg white
  • VMJ1 146-70 was determined using hemoglobine as substrate described above and was 13300 U / g formulated liquid product. 1 % enzyme compares to 133000 U / kg egg white.
  • the egg white was centrifuged for 10 minutes at 5.000 rpm to remove the yeast. The supernatant was used for analysis and pasteurization followed by gelling. The gel points were measured twice; the values for the increase in gel point compared to reference egg white are presented in Table 6.
  • Table 6 Difference in gelling temperature of desugared egg white treated with Aspergillopepsin II and untreated desugared egg white at pH 5.6
  • Aspergillopepsin II is effective to increase the egg white gel point with about 5°C. The incubation can take place during desugaring of egg white.
  • SDS PAGE SDS page showed that during treatment of egg white with aspergillopepsin II the proteins of between about 45 and 60 kDa (ovalbumin, globulins) remained mostly intact. Moreover, also the protein band of 65-80 kDa (ovotransferin) remained mostly intact. As the larger proteins remained mostly intact the gel strength remained substantial.
  • Example 7 Treatment of egg white with different doses of Validase BNP-L (EC3.4.24.28) during desugaring of egg white with Validase BNP

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  • Food Science & Technology (AREA)
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Abstract

La présente invention concerne un procédé de préparation d'une composition de blanc d'œuf, comprenant l'incubation de blanc d'œuf avec une protéase, de façon à préparer une composition de blanc d'œuf qui présente une température de gélification accrue par rapport à celle de blanc d'œuf n'ayant pas été incubé avec la protéase, et la préparation de la composition de blanc d'œuf.
PCT/EP2012/057767 2011-04-29 2012-04-27 Préparation d'une composition de blanc d'œuf Ceased WO2012146717A1 (fr)

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Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2015092098A1 (fr) * 2013-12-20 2015-06-25 Consejo Superior De Investigaciones Cientificas (Csic) Compositions alimentaires saines présentant des textures de gel ou de mousse et comprenant des produits à base d'œufs hydrolysés
WO2016032352A1 (fr) 2014-08-28 2016-03-03 Romvac Company Sa Fabrication et utilisation d'ovotransferrine moderne (otf-m)
CN105813474A (zh) * 2013-12-11 2016-07-27 帝斯曼知识产权资产管理有限公司 治疗先天免疫应答疾病的药物和方法
CN106572680A (zh) * 2014-05-28 2017-04-19 天野酶株式会社 高乳化性蛋清水解物
CN107581526A (zh) * 2017-10-10 2018-01-16 四川理工学院 一种高弹、高透明蛋制品的生产方法
CN108782943A (zh) * 2018-07-02 2018-11-13 福建农林大学 一种提高卵白蛋白的起泡性以及乳化性的方法
WO2022048857A1 (fr) * 2020-09-03 2022-03-10 Interlaap Corporation Blanc d'œuf buvable
WO2023183402A1 (fr) * 2022-03-22 2023-09-28 Isonova Technologies Llc Procédé pour séparer la matière grasse et les protéines dans des oeufs et des produits à base d'oeufs

Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS61149071A (ja) * 1984-12-24 1986-07-07 House Food Ind Co Ltd 加工卵白の製造法
JPS6314681A (ja) * 1986-07-07 1988-01-21 Eisai Co Ltd 卵白酵素分解物の製造方法
WO2002068623A2 (fr) 2001-02-23 2002-09-06 Dsm Ip Assets B.V. Nouveaux genes codant les nouvelles enzymes proteolytiques
WO2005074703A1 (fr) * 2004-02-10 2005-08-18 Join Co. Ltd Procede de preparation d'un liquide a base de blanc d'oeuf pour la prevention de la coagulation due a un traitement thermique
JP2006101801A (ja) * 2004-10-07 2006-04-20 Q P Corp 耐熱性卵白
JP2007053932A (ja) * 2005-08-23 2007-03-08 Taiyo Kagaku Co Ltd 清澄性の高い卵白加水分解物の製造方法

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS61149071A (ja) * 1984-12-24 1986-07-07 House Food Ind Co Ltd 加工卵白の製造法
JPS6314681A (ja) * 1986-07-07 1988-01-21 Eisai Co Ltd 卵白酵素分解物の製造方法
WO2002068623A2 (fr) 2001-02-23 2002-09-06 Dsm Ip Assets B.V. Nouveaux genes codant les nouvelles enzymes proteolytiques
WO2005074703A1 (fr) * 2004-02-10 2005-08-18 Join Co. Ltd Procede de preparation d'un liquide a base de blanc d'oeuf pour la prevention de la coagulation due a un traitement thermique
JP2006101801A (ja) * 2004-10-07 2006-04-20 Q P Corp 耐熱性卵白
JP2007053932A (ja) * 2005-08-23 2007-03-08 Taiyo Kagaku Co Ltd 清澄性の高い卵白加水分解物の製造方法

Non-Patent Citations (6)

* Cited by examiner, † Cited by third party
Title
DATABASE WPI Week 198633, 1986 Derwent World Patents Index; AN 1986-216605, XP002658158 *
J. FOOD ENGINEERING, vol. 83, 2007, pages 404 - 413
NIELSEN P.M. ET AL.: "Improved Method for Determining Food Protein Degree of Hydrolysis", JOURNAL OF FOOD SCIENCE, vol. 66, no. 5, 2001, XP055204159
NIELSEN, J. FOOD SCIENCE, vol. 66, no. 5, 2001, pages 642 - 646
V. LECHEVALIER, J. FOOD ENG., vol. 83, 2007, pages 404 - 413
Y. MINE, TRENDS IN FOOD SCI TECHN., vol. 6, 1995, pages 225 - 232

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CN105813474A (zh) * 2013-12-11 2016-07-27 帝斯曼知识产权资产管理有限公司 治疗先天免疫应答疾病的药物和方法
US10413599B2 (en) 2013-12-11 2019-09-17 Dsm Ip Assets B.V. Medicament and method for treating innate immune response diseases
US9648897B2 (en) 2013-12-20 2017-05-16 Consejo Superior De Investigaciones Cienfificas Healthy food compositions having gel or foam textures and comprising hydrolyzed egg products
ES2539735A1 (es) * 2013-12-20 2015-07-03 Consejo Superior De Investigaciones Científicas (Csic) Composiciones alimentarias saludables que presentan texturas de gel o espuma y que comprenden ovoproductos hidrolizados
WO2015092098A1 (fr) * 2013-12-20 2015-06-25 Consejo Superior De Investigaciones Cientificas (Csic) Compositions alimentaires saines présentant des textures de gel ou de mousse et comprenant des produits à base d'œufs hydrolysés
JP2015130856A (ja) * 2013-12-20 2015-07-23 コンセホ・スペリオール・デ・インベスティガシオネス・シエンティフィカス ゲルまたは泡のテクスチャーを有し、加水分解された卵製品を含む健康食品組成物
ES2539203A1 (es) * 2013-12-20 2015-06-26 Consejo Superior De Investigaciones Científicas Composiciones alimentarias saludables que presentan texturas de gel o espuma y que comprenden ovoproductos hidrolizados
US12599150B2 (en) 2014-05-28 2026-04-14 Amano Enzyme Inc. Highly emulsifiable albumen hydrolysate
CN106572680A (zh) * 2014-05-28 2017-04-19 天野酶株式会社 高乳化性蛋清水解物
JPWO2015181917A1 (ja) * 2014-05-28 2017-04-20 天野エンザイム株式会社 高乳化性卵白加水分解物
EP3155902A4 (fr) * 2014-05-28 2017-12-06 Amano Enzyme Inc. Hydrolysat d'albumine fortement émulsifiable
CN106572680B (zh) * 2014-05-28 2020-03-17 天野酶株式会社 高乳化性蛋清水解物
WO2016032352A1 (fr) 2014-08-28 2016-03-03 Romvac Company Sa Fabrication et utilisation d'ovotransferrine moderne (otf-m)
CN107581526A (zh) * 2017-10-10 2018-01-16 四川理工学院 一种高弹、高透明蛋制品的生产方法
CN108782943A (zh) * 2018-07-02 2018-11-13 福建农林大学 一种提高卵白蛋白的起泡性以及乳化性的方法
EP4208039B1 (fr) * 2020-09-03 2024-08-21 Interlaap Corporation Blanc d'oeuf buvable
WO2022048857A1 (fr) * 2020-09-03 2022-03-10 Interlaap Corporation Blanc d'œuf buvable
US12635716B2 (en) 2020-09-03 2026-05-26 Interlaap Corporation Drinkable egg white
WO2023183402A1 (fr) * 2022-03-22 2023-09-28 Isonova Technologies Llc Procédé pour séparer la matière grasse et les protéines dans des oeufs et des produits à base d'oeufs

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