WO2000018249A1 - Procede pour reguler la glycosylation de type maillard des proteines de lactoserum et produits ayant des proprietes fonctionnelles accrues - Google Patents

Procede pour reguler la glycosylation de type maillard des proteines de lactoserum et produits ayant des proprietes fonctionnelles accrues Download PDF

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Publication number
WO2000018249A1
WO2000018249A1 PCT/NZ1999/000163 NZ9900163W WO0018249A1 WO 2000018249 A1 WO2000018249 A1 WO 2000018249A1 NZ 9900163 W NZ9900163 W NZ 9900163W WO 0018249 A1 WO0018249 A1 WO 0018249A1
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WIPO (PCT)
Prior art keywords
whey protein
glycation
process according
product
acid
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PCT/NZ1999/000163
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English (en)
Inventor
Michael John Boland
Jeremy Paul Hill
Kerianne Carol Higgs
Neill Ward Haggarty
Maria Estela Puchulu Campanella
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New Zealand Dairy Research Institute
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Priority to AU58873/99A priority Critical patent/AU5887399A/en
Priority to NZ510680A priority patent/NZ510680A/en
Publication of WO2000018249A1 publication Critical patent/WO2000018249A1/fr

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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
    • A23J3/04—Animal proteins
    • A23J3/08—Dairy proteins
    • 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
    • A23L27/20—Synthetic spices, flavouring agents or condiments
    • A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
    • A23L27/215—Synthetic spices, flavouring agents or condiments containing amino acids heated in the presence of reducing sugars, e.g. Maillard's non-enzymatic browning
    • 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
    • A23L27/66—Use of milk products or milk derivatives in the preparation of dressings
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • This invention relates to a dairy product and process, particularly although by no means exclusively, to a process of controlling Maillard-type glycation of whey proteins to produce a product having enhanced functional properties.
  • the Maillard reaction which occurs even at low temperatures, has been extensively studied since 1912 (Maillard, 1912).
  • the Maillard reaction is a complex group of many reactions occurring "'in vivo" as well as during processing and storage. The reaction is pH and temperature dependent. It is also affected by relative humidity /water activity of the samples, reducing sugar and metal ions.
  • the first irreversible product originated by the non-enzymatic interaction of a saccharide/carbonyl group and the or e-amino groups of proteins is known as the Amadori compound.
  • the Amadori compound can be formed by many reducing sugars. oligosaccharides and their derivatives. Examples are e-lactosyl-lysine, fructosyl-lysine or tagatosyl-lysine. All of these compounds under acid hydrolysis generate furosine. Quantitation of furosine is therefore an excellent way of monitoring the extent of modification of proteins due to the Maillard reaction (Erbersdobler, 1986).
  • Watanabe et al (1984) showed altered heat stability of whey protein preparations as well as an isolated ⁇ -lactalbumin and ⁇ -lactoglobulin whereby glycation with lactose increased the temperature of denaturation and coagulation of these protein preparations.
  • MRP Maillard reaction products
  • Morgan et al (1997) and Leonil et al (1997) characterised the adducts formed by lactose and ⁇ -lactoglobulin during mild heat treatment.
  • Leonil et al (1997) evaluated the extent of the early Maillard reaction by mass spectrometry and provided the first direct evidence of specific lactosylation of ⁇ -lactoglobulin.
  • Morgan et al (1998) monitored Amadori product formulation between lactose and ⁇ -lactoglobulin directly using electrospray ionisation mass spectrometry and found the glycation reaction was faster at lower water activity, and further observed different heterogenous ⁇ -lactoglobulin glycoforms.
  • step ii) subjecting the whey protein-containing material of step i) to Maillard-type glycation reaction by incubation of the whey protein-containing material with a reducing sugar under controlled temperature and moisture conditions for a sufficient time to produce a desired level of glycation without causing denaturation of the whey protein; iii) terminating the Maillard-type reaction after a desired level of glycation has been reached and removing any excess reducing sugars; and
  • the preferred reaction conditions enable the reaction to proceed efficiently to produce a whey protein product having enhanced functional properties on a commercially viable scale.
  • the reaction is preferably carried out at a ratio of lg whey protein: 0.02-0.6g reducing sugar, water activity of 0.3-0.8a w and temperature of 30-75°C for 18-240 hours.
  • the water activity is preferably 0.6 a w .
  • the temperature is preferably held at between 40°C and 50°C.
  • the reaction is terminated at the required degree of glycation in step iii) by further drying the powder to a water activity of less than 0.20 and reducing the temperature to 20°C or below.
  • step ii) is carried out at a pH of between 6.0-8.0.
  • the process may be precisely controlled by monitoring the level of glycation by mass spectrometry or any other method known in the art, such as, for example, by monitoring the production of furosine, in order to produce a product having the desired level of glycation and therefore, the desired enhanced functional properties.
  • an additional step of monitoring the rate of glycation by monitoring the production of furosine may be carried out before step iii) and the reaction terminated once glycation has proceed to a desired level.
  • the whey protein-containing material may comprise one or more of the following: whey protein isolate (WPI), whey protein concentrate (WPC), whey powder, milk protein concentrate (MPC), milk protein isolate (MPI) and skim and whole milk powder.
  • WPI whey protein isolate
  • WPC whey protein concentrate
  • MPC milk protein concentrate
  • MPI milk protein isolate
  • skim and whole milk powder The reducing sugar may comprise one or more of the following: lactose, glucose, galactose, maltose, fructose or their derivatives including glucose-6-phosphate, gluconic acid, or any oligosaccharide or saccharide conjugate that contains a reducing sugar.
  • the glycated whey protein product has one or more enhanced functional properties selected from the group comprising enhanced heat stability, emulsifying activity, foamability, antioxidant activity and enterotoxin binding capacity.
  • the invention provides a process for enhancing the functional properties of stored dairy powder products comprising the steps:
  • the stored dairy powder product may comprise WPC, WPI, whey powder, MPC, MPI and skim or whole milk powders.
  • the conditions for optimal glycation may comprise:
  • the pH of the dairy powder product is also between pH 6.0-8.0.
  • the reducing sugar may be inherently present in the dairy powder product or it may be added.
  • the reducing sugar is present in a ratio of 1.0g whey protein: 0.02-0.6g reducing sugar.
  • the reducing sugar is selected from one or more of lactose, glucose, galactose, maltose, fructose or their derivatives on any oligosaccharide or saccharide conjugate that contains a reducing sugar.
  • the time sufficient to provide a desired level of glycation in step ii) is between 1 hour and 80 days.
  • the conditions in step iii) which will inhibit further glycation include the reduction of temperature to below 20°C and/or the reduction of water activity to below 0.2a w .
  • the stored dairy products treated according to this process and maintained under conditions which inhibit further glycation do not suffer from the phenomenon of 'browning' that occurs in stored dairy powder products due to extensive Maillard reaction.
  • the enhanced functional properties of the stored dairy powders includes one or more of the following: enhanced heat stability, emulsifying activity, antioxidant activity and enterotoxin binding capacity.
  • the invention provides a whey protein-containing dairy product wherein the whey protein has been glycated to a desired level according to the process of the invention to provide enhanced functional properties to the product.
  • the whey protein- containing dairy product may comprise WPI, WPC, whey powder, MPC, MPI, skim and whole milk products.
  • the enhanced functional properties of the dairy product include one or more of the following: enhanced heat stability, emulsifying activity, antioxidant activity and enterotoxin binding capacity.
  • the dairy product is used as an additive to improve the functionality and nutritional content of foodstuffs.
  • the product is used as an additive in clear acid beverages, especially in citric acid, phosphoric acid, lactic acid, malic acid and gluconic acid beverages where the glycated product improves the heat stability of the acid beverage formulations.
  • the product may also be used as an additive in the formulation of low fat salad dressing where the improved emulsification properties are of particular use.
  • the present invention provides for the use of a glycated whey protein- containing material according to the invention in the production of an enhanced functional foodstuff.
  • the present invention provides for a foodstuff containing a glycated whey protein-containing material according to the invention.
  • the foodstuff is an acid beverage or low fat salad dressing.
  • the present invention provides a modified whey protein-containing material comprising a desired level of glycated whey protein having one or more enhanced functional properties.
  • the whey protein material may be selected from WPI, WPC, whey powder, MPI, and skim or whole milk powder.
  • the functional properties are as defined above and the modified whey protein may be useful as a food additive as described above for the dairy product of the invention.
  • Figures 1 and 2 show mass spectrometer time courses for the glycation of ⁇ -lactoglobulin in lactose supplemented WPI samples.
  • Figure 3 shows a fhermogram of control and glycated whey protein-containing material.
  • Figure 4 shows the pH dependent emulsifying properties of glycated and control whey protein-containing material.
  • Figures 5 and 6 show acid heat stabilities of control and glycated whey protein- containing material.
  • Figure 7 shows the mass spectrum of ⁇ -lactoglobulin in a WPI after glycation for 6 days at 40°C with a protein to lactose ratio of 1 :0. l(w/w).
  • Figure 8 shows mass spectra for ⁇ -lactoglobulin in a WPI after glycation for 18 h at 50°C with protein to lactose ratios of l :0.1(w/w) and l :0.4(w/w).
  • Figure 9 - shows mass spectra for ⁇ -lactoglobulin in a WPC after glycation for 0 and 2 days.
  • Figure 10 shows mass spectra for ⁇ -lactoglobulin in a lactose supplemented WPI after glycation for 0 and 10 days.
  • Figures 1 1 & 12 show mass spectra for ⁇ -lactoglobulin in WPC samples glycated by manipulating storage conditions.
  • Figures 13-15 show mass spectra for ⁇ -lactoglobulin in WPC samples glycated by manipulating storage conditions.
  • Figure 16 shows the distribution of glycoforms before and after lactosylation at
  • the mixture was dissolved in 400ml MilliQ water and dialysed for 48h using a 10,000 molecular weight cut off dialysis tubing (Union Carbide) against distilled water.
  • the dialysed solution was then ultraf ⁇ ltered using a YM10 membrane (Amicon). The retentate was then dried.
  • the nitrogen content was determined by the Dumas principle using a Leco FP-2000, Leco Corporation, St Joseph, Michigan, USA.
  • the number of reacted lysines in the protein was estimated by measuring furosine by an adaption of the method of Henle et al (1995).
  • the level of the early Maillard Amadori compound lactulosyl-lysine was calculated by multiplying the furosine value by 2.25 (the factor 2.25 accounts for the yield of furosine from the Amadori product (Molnar-Perl & Pinter-Szakacs, 1986)).
  • the amount of lysine in the product was estimated as 12 g/lOOg.
  • Table 1 shows the results for furosine measurements, and the equivalent percentage of reacted lysine amino groups calculated from the furosine results, for the two WPI samples.
  • the controls showed that the two WPI samples had different initial levels of lactosylated lysines. This was due to the different processing histories of the samples.
  • the results for the 240h (10 days) of lactosylation showed that the sample with the higher initial level of lactosylation (WPI-2) had a much higher percentage of lysines reacted at the end of the 240h incubation period. This indicates that the initial level of lactosylation of any whey protein-containing powder, to be used for controlled lactosylation, must be predetermined. lactosylated lysines. This was due to the different processing histories of the samples.
  • the results for the 240h (10 days) of lactosylation showed that the sample with the higher initial level of lactosylation (WPI-2) had a much higher percentage of lysines reacted at the end of the 240h incubation period. This indicates that the initial level of lactosylation of any whey protein-containing powder, to be used for controlled lactosylation, must be predetermined.
  • Whey protein isolate is a rich source of lysine (approximately 12g/100g) and although 43.6% of the lysines are blocked in WPI-2A, the product still has 7g/100g of available lysine, a value very close-to caseinate, which is considered a good source of lysine (8g/100g).
  • Figure 1 shows the results for WPI-1 at Oh, 168h (7 days) and 240h (10 days).
  • a and B refer to ⁇ -lactoglobulin variants A and B.
  • At Oh very little lactosylation is detected and the major peaks are the native ⁇ -lactoglobulin variants A and B.
  • After 7 days adducts of 1-4 lactosyl-ly sines are seen (llac-41ac) with incremental mass increases of 324 Daltons (the molecular weight of lactose) to the molecular mass of the native ⁇ - lactoglobulin variants A and B (WPI-1 A).
  • the thermal behaviour of WPI-1 was studied with a Perkin-Elmer DSC-7 differential scanning calorimeter. Selected samples were desalted using Centricon micro concentrators with a 3000 molecular weight cut-off. Aliquots of lO ⁇ L of a 10% protein solution (w/w), in simulated milk ultrafiltrate (Jenness & Koops, 1962) were taken and sealed in stainless steel capsules. The weight of the pans was measured before and after analysis. All analyses were performed in duplicate. The scanning temperature range was 30-115°C at a heating rate of 10°C/min. The onset and denaturation temperature as well as denaturation enthalpies were calculated from the thermogram using a Perkin-Elmer Pyris DSC software data analyser.
  • Figure 3 shows the enhanced heat stability of the lactosylated WPI (WPI- IB) compared to the original WPI control (WPI-1). This is demonstrated by the higher onset (onset temp) and denaturation temperature (Td). Values for the onset temp, Td, ⁇ T, ⁇ (measurement of the cooperativity for protein aggregation) and ⁇ H (total energy required to denature the protein mixture) are shown in Table 2.
  • the emulsifying ability was tested using a Labplant jet homogenizer (Labplant, Huddersfield, UK) as outlined in the manufacturers handbook. A known mass of protein product was dissolved in 100ml of buffer at 55 °C in a shaking water bath.
  • the weight of protein used was sufficient to give a protein content in the final emulsion of 0.5wt%.
  • the solutions were held at 55°C for 1 hour. At the same time a portion of soya oil was heated to 55°C.
  • the buffers used were citric acid- disodium hydrogen phosphate (Mcllvaine) buffers at pH 3.6, 4.0 and 6.8. All emulsions were made up at 20wt% soya oil.
  • FIG. 4 shows the mean d 32 for the non- lactosylated (WPI-1) and the lactosylated WPI (WPI- IB) at the three pH values.
  • a smaller value of d 3 , 2 means that the protein is a better emulsifier.
  • the emulsifying properties of whey proteins show a relatively complex pH dependence. A minimum is observed in the emulsifying properties at the isoelectric point (pi). This can be attributed to the minimum in protein solubility that occurs at that pH value.
  • the emulsifying properties improve, although generally the emulsifying activity at pH values below the pi is lower than at pH values above the pi.
  • the glycated whey protein isolate showed a marked improvement in emulsifying ability (smaller particle size) at pH 4.0. This is probably a result of a change in the pi caused by blockage of positively charged lysine side chains by reaction with sugar residues.
  • WPI-1 A and WPI- IB in heated systems adjusted with (a) citric acid and (b) phosphoric acid.
  • FIG 5 shows clearly that lactosylation has increased the acid stability of WPI-1 (as measured by absorbance at 610nm) in both (a) citric acid and (b) phosphoric acid ( Figure 2).
  • the increase in acid-heat stability was particularly large at pH 4.0 and pH 4.2.
  • the pH 4.2 results shown for citric acid had reached the maximum turbidity measurable at 610nm (3.0) and the samples had precipitated.
  • Figure 8 shows the mass spectrometer time course for two experiments using WPI-2 at 50°C.
  • One experiment used a lactose to protein ratio of 0.7: 1 (w/w) and the other a lactose to protein ratio of 0.4: l(w/w).
  • Increasing the temperature decreased the time required for the glycation to 18 hours.
  • the a w for this experiment was 0.6. 2 GLYCATION OF WPC
  • Glycation of a standard 56% protein WPC (ALACEN 421, New Zealand Milk Products) was performed at 40°C under controlled conditions of a w (0.7).
  • the WPC contained 34% lactose, which gave a lactose:protein ratio of 0.6: l(w/w).
  • the a w of the product was adjusted to 0.7 to carry out the glycation.
  • the reaction was monitored by mass spectrometry.
  • Figure 9 shows the mass spectrometry results for the lactosylation of ALACEN 421.
  • the product already contains lactosylated ⁇ -lactoglobulin derivatives, with up to 3 adducts detected. As before this is due to the processing history of the product. After two days a product with 8 adducts is produced with the mean around 4 or 5 adducts. This product could form the feed to a process to produce a lactosylated WPI with enhanced functionalities.
  • the reaction conditions selected in the present invention enable the reaction to proceed efficiently to produce a whey protein product having enhanced functional properties on a commercially viable scale.
  • whey protein reducing sugar eg 1.0:0.1
  • the sugar is completely consumed in the reaction and there is no need for removal of excess sugar.
  • the reaction proceeds rapidly, but the excess of sugar that remains after the desired degree of glycation desired is achieved must be removed. If not the reaction will proceed to the latter stages of the Maillard reaction and undesirable properties will appear (browning, off flavours, lack of functionality etc).
  • the reaction proceeds very slowly.
  • the temperature range it has been found that below 30°C the reaction proceeds very slowly and above 75°C other reactions can take place that are detrimental to protein functionality.
  • Dairy powders (56 % WPC, 80% WPC, Skim Milk powder, Whole Milk powder and Milk Protein Concentrate) were stored at 30, 35 and 40 °C under controlled water activities (a of 0.33, 0.72 and 0.79. Samples were removed at various time intervals between 4 h and 36 days for analysis. The glycation process was monitored by either mass spectroscopy, measurement of furosine (Table 3) or measurement of available amine.
  • Glycation of dairy powders is possible under a variety of conditions and can be controlled by manipulating the storage conditions of products containing reducing sugars.
  • the examples given show a range of both storage conditons and powders.
  • the present invention provides a process for producing a glycated whey protein product and glycated whey protein products per se which have enhanced functional properties useful as food additives to improve functionality and nutritional content of foodstuffs.
  • a process for producing a glycated whey protein product and glycated whey protein products per se which have enhanced functional properties useful as food additives to improve functionality and nutritional content of foodstuffs.
  • industrial applicability is the use of the glycated whey protein product in clear acid beverage formulations.
  • Whey improves oxidative stability of soybean oil.
  • Antibody response to haptenic sugar antigen immunodominancy of protein-bound lactose formed by aminocarbonyl reaction. Molecular Immunology, 24, 421-425.
  • Nonenzymatic lactosylation of bovine ⁇ -lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms.

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  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
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Abstract

Cette invention se rapporte à un procédé pour réguler la glycosylation de type Maillard d'une substance contenant des protéines de lactosérum, afin d'accroître leurs propriétés fonctionnelles, ainsi qu'à des produits protéiques de lactosérum glycosylés en soi, et à leur utilisation comme additifs alimentaires, en vue d'améliorer la fonctionnalité et la teneur nutritive de denrées alimentaires.
PCT/NZ1999/000163 1998-09-28 1999-09-28 Procede pour reguler la glycosylation de type maillard des proteines de lactoserum et produits ayant des proprietes fonctionnelles accrues WO2000018249A1 (fr)

Priority Applications (2)

Application Number Priority Date Filing Date Title
AU58873/99A AU5887399A (en) 1998-09-28 1999-09-28 Process for controlling maillard-type glycation of whey proteins and products with enhanced functional properties
NZ510680A NZ510680A (en) 1998-09-28 1999-09-28 Process for controlling maillard-type glycation of whey proteins and products with enhanced functional properties

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NZ332080 1998-09-28
NZ33208098 1998-09-28

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WO2000018249A1 true WO2000018249A1 (fr) 2000-04-06

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WO2006053642A1 (fr) * 2004-11-16 2006-05-26 Blattmann Cerestar Ag Ingredients alimentaires proteiques et procede pour les modifier chimiquement
WO2006065135A2 (fr) * 2004-12-15 2006-06-22 Csm Nederland B.V. Proteines modifiees avec des proprietes alterees d'agregation
WO2007054587A1 (fr) * 2005-11-14 2007-05-18 Nestec S.A. Promotion de tolerance orale a base de proteines glycatees
EP1800544A1 (fr) * 2005-12-23 2007-06-27 Stichting Technologisch Top-Instituut Voedselwetenschappen Gélification controllée d'un mélange de protéines par glycosylation.
EP2025235A1 (fr) * 2007-08-08 2009-02-18 Stichting Top Institute Food and Nutrition Utilisation de protéine globulaire conjugués d'oligasaccharide
WO2009117572A1 (fr) * 2008-03-19 2009-09-24 Wisconsin Alumni Research Foundation Production de conjugués protéine-polysaccharide
US7687095B2 (en) 2005-09-30 2010-03-30 Kraft Foods Global Brands Llc High moisture, low fat cream cheese with maintained product quality and method for making same
AU2005324026B2 (en) * 2005-01-06 2011-10-20 Nestec S.A. Milk powder
WO2013067603A1 (fr) * 2011-11-10 2013-05-16 Clover Corporation Limited Encapsulation de compléments d'ingrédients alimentaires de produits pharmaceutiques
WO2013132265A2 (fr) 2012-03-09 2013-09-12 Nandi Proteins Limited Procédé pour modifier des protéines
CN104970185A (zh) * 2015-04-09 2015-10-14 山东农业大学 高凝胶强度大豆分离蛋白的加工方法
CN105104706A (zh) * 2015-04-09 2015-12-02 山东农业大学 高乳化活性大豆分离蛋白的加工方法
EP3384779A1 (fr) * 2017-04-05 2018-10-10 Institut National De La Recherche Agronomique (INRA) Particules d'agrégat de protéines stabilisées et procédé pour la préparation desdites particules
CN109717428A (zh) * 2019-03-12 2019-05-07 江南大学 一种富含阿马多瑞化合物的果蔬粉及制备方法
WO2020150298A1 (fr) * 2019-01-15 2020-07-23 University Of Georgia Research Foundation, Inc. Produits alimentaires de glycation précoce pour le traitement et la prévention de maladies auto-immunes
CN111758832A (zh) * 2020-07-10 2020-10-13 宜春学院 一种低致敏性乳清蛋白的制备方法
WO2021202989A1 (fr) * 2020-04-03 2021-10-07 Atomo Coffee, Inc. Substrats végétaux soumis à la réaction de maillard croisée
WO2022251529A1 (fr) * 2021-05-26 2022-12-01 Atomo Coffee, Inc. Substrats végétaux soumis à une réaction de maillard croisée
CN115606800A (zh) * 2022-07-23 2023-01-17 深圳大学 一种高稳定性高载量糖基化蛋白纤维纳米递送体系的构建方法

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Cited By (32)

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Publication number Priority date Publication date Assignee Title
WO2006053642A1 (fr) * 2004-11-16 2006-05-26 Blattmann Cerestar Ag Ingredients alimentaires proteiques et procede pour les modifier chimiquement
WO2006065135A2 (fr) * 2004-12-15 2006-06-22 Csm Nederland B.V. Proteines modifiees avec des proprietes alterees d'agregation
WO2006065135A3 (fr) * 2004-12-15 2006-08-31 Wageningen Ct For Food Science Proteines modifiees avec des proprietes alterees d'agregation
JP2008523803A (ja) * 2004-12-15 2008-07-10 シーエスエム ネーダーランド ビー．ブイ． 凝集特性を変化させた修飾タンパク質
US8329240B2 (en) 2005-01-06 2012-12-11 Nestec S.A. Milk powder
AU2005324026B2 (en) * 2005-01-06 2011-10-20 Nestec S.A. Milk powder
US7687095B2 (en) 2005-09-30 2010-03-30 Kraft Foods Global Brands Llc High moisture, low fat cream cheese with maintained product quality and method for making same
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JP2009515929A (ja) * 2005-11-14 2009-04-16 ネステク ソシエテ アノニム 糖化タンパク質を用いた経口免疫寛容促進
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