Hydrolyzed vegetable protein

Last updated

Hydrolyzed vegetable protein (HVP) products are foodstuffs obtained by protein hydrolysis and are used as ingredients to create a bouillon (broth) taste without the vegetables, bones, simmering, or other standard elements of creating bouillon from scratch.

Contents

Regarding the production process, a distinction can be made between acid-hydrolyzed vegetable protein (aHVP), enzymatically produced HVP, and other seasonings, e.g., fermented soy sauce. Hydrolyzed vegetable protein products are particularly used to round off the taste of soups, sauces, meat products, snacks, and other dishes, as well as for the production of ready-to-cook soups and bouillons.

History

Food technologists have long known that protein hydrolysis produces a meat bouillon-like odor and taste. [1] Hydrolysates have been a part of the human diet for centuries, notably in the form of fermented soy sauce, or Shoyu. Shoyu, traditionally made from wheat and soy protein, has been produced in Japan for over 1,500 years, following its introduction from mainland China. The origins of producing these materials through the acid hydrolysis of protein (aHVP) can be traced back to the scarcity and economic challenges of obtaining meat extracts during the Napoleonic wars. [2]

In 1831, Berzelius obtained products having a meat bouillon taste when hydrolysing proteins with hydrochloric acid. [3] Julius Maggi produced acid-catalyzed hydrolyzed vegetable protein industrially for the first time in 1886. [4]

In 1906, Fischer found that amino acids contributed to the specific taste. [5] In 1954, D. Phillips found that the bouillon odor required the presence of proteins containing threonine. [6] Another important substance that gives a characteristic taste is glutamic acid.

Manufacture

Almost all products rich in protein are suitable for the production of HVP. Today, it is made mainly from protein resources of vegetable origin, such as defatted oil seeds (soybean meal, grapeseed meal) and protein from maize (Corn gluten meal), wheat (gluten), pea, and rice. [7] The process and the feedstock determines the organoleptic properties of the end product. Proteins consist of chains of amino acids joined through amide bonds. When subjected to hydrolysis (hydrolyzed), the protein is broken down into its component amino acids.

In aHVP, hydrochloric acid is used for hydrolysis. The remaining acid is then neutralized by mixing with an alkali such as sodium hydroxide, which leaves behind table salt, which comprises up to 20% of the final product (acid-hydrolyzed vegetable protein, aHVP).

In enzymatic HVP (eHVP), proteases are used to break down the proteins under a more neutral pH and lower temperatures. [8] The amount of salt is greatly reduced.

Because of the different processing conditions, the two types of HVP have different sensory profiles. aHVP is usually dark-brown in color and has a strong savory flavor, whereas eHVP usually is lighter in color and has a mild savory flavor. [9] [10]

Acid hydrolysis

Acid hydrolysates are produced from various edible protein sources, with soy, corn, wheat, and casein being the most common. For the production of aHVP, the proteins are hydrolyzed by cooking with a diluted (15–20%) hydrochloric acid, at a temperature between 90 and 120 °C for up to 8 hours. After cooling, the hydrolysate is neutralized with either sodium carbonate or sodium hydroxide to a pH of 5 to 6. During hydrolysis, extraneous polymeric material known as humin, which forms from the interaction of carbohydrate and protein fragments, is generated and subsequently removed by filtration and then further refined. [11]

The source of the raw material, concentration of the acid, the temperature of the reaction, the time of the reaction, and other factors can all affect the organoleptic properties of the final product. Activated carbon treatment can be employed to remove both flavor and color components, to the required specification. Following a final filtration, the aHVP may, depending upon the application, be fortified with additional flavoring components. Thereafter, the product can be stored as a liquid at 30–40% dry matter, or alternatively it may be spray dried or vacuum dried and further used as a food ingredient. [11]

One hundred pounds (45kg) of material containing 60% protein will yield 100 pounds of aHVP, which contains approximately 40 pounds (18 kg) of salt. This salt gain occurs during the neutralization step. [2]

Enzymatic hydrolysis

For the production process of enzymatic HVP, enzymes are used to break down the proteins. To break down the protein to amino acids, proteases are added to the mixture of defatted protein and water. Due to the sensitivity of enzymes to a specific pH, either an acid or a base is added to match the optimum pH. Depending on the activity of the enzymes, up to 24 hours are needed to break down the proteins. The mixture is heated to inactivate the enzymes and then filtered to remove the insoluble carbohydrates (humin).

Since no salt is formed during the production process, manufacturers may add salt to eHVP preparations to extend shelf life or to provide a product similar to conventional aHVP.

Composition

Liquid aHVP typically contains 55% water, 16% salt, 25% organic substances (thereof 20% protein (amino acids) analyzed as about 3% total nitrogen and 2% amino nitrogen).

Many amino acids have either a bitter or sweet taste. In many commercial processes, nonpolar amino acids such as L-leucine and L-isoleucine are often removed to create hydrolysates with a more mellow and less bitter character. D-tryptophan, D-histidine, D-phenylalanine, D-tyrosine, D-leucine, L-alanine, and glycine are known to be sweet, while bitterness is associated with L-tryptophan, L-phenylalanine, L-tyrosine, and L-leucine. [2] [12]

Tyrosine is an amino acid susceptible to halogenation during hydrolysis with HCl. To prevent this, phenol is often added to the solution. [13] High fat content can also reduce tyrosine yields, but this can be overcome by defatting samples prior to acid hydrolysis. [14]

Lysine is stable under standard acid hydrolysis conditions, and, in pure proteins and foods thermally untreated, can be readily determined using HCl hydrolysis. Problems appear when foods are processed, especially those subjected to heat treatment, as the side-chain amino group can react with other compounds, such as reducing sugars, producing Maillard products. [15] Some of the Maillard products are acid labile and will revert back to lysine, [16] and different other compounds, [17] leading to an overestimation of lysine content.

The organoleptic properties of HVP is determined not only by amino acid composition, but also by the various aroma-bearing substances other than amino acids created during the production of both aHVP and eHVP. Aromas can be formed via amino acid decomposition, Maillard reaction, sugar cyclization, and lipid oxidation. [18] A complex mix of aromas similar to butter, meat, [19] [18] bone stock, [18] wood smoke, [20] lovage/Maggi seasoning, [21] and many other substances can be produced, depending on reaction conditions (time, temperature, hydrolysis method, additional feedstock such as xylose and spices). [18] [22]

According to the European Code of Practice for Bouillons and Consommés, hydrolyzed protein products intended for retail sale correspond to these characteristics: [23]

Use

When foods are produced by canning, freezing, or drying, some flavor loss is almost inevitable. Manufacturers can use HVP to make up for it. [7] Therefore, HVP is used in a wide variety of products such as in the spice, meat, fish, fine-food, snack, flavor, and soup industries.

Safety

3-MCPD

3-MCPD, a carcinogen in rodents and a suspected human carcinogen, is created during acid-hydrolysis as glycerol released from lipid (e.g. triglycerides) reacts with hydrochloric acid. Legal limits have been set to keep aHVP products safe for human consumption. aHVP manufacturers can reduce the amount of 3-MCPD to acceptable limits by (1) careful control of reaction time and temperature (2) timely neutralization of hydrochloric acid, optionally extending to an alkaline hydrolysis step to destroy any 3-MCPD already formed (3) replacement of hydrochloric acid with other acids such as sulfuric acid. [11]

As an allergen

Whether hydrolyzed vegetable protein is an allergen or not is contentious.

According to European law, wheat and soy are subject to allergen labelling in terms of Regulation (EU) 1169/2011 on food information to consumers. Since wheat and soy used for the production of HVP are not exempted from allergen labelling for formal reasons, HVP produced by using those raw materials has to be labelled with a reference to wheat or soy in the list of ingredients.

Nevertheless, strong evidence indicates at least aHVP is not allergenic, since proteins are degraded to single amino acids which are not likely to trigger an allergic reaction. An 2010 study has shown that aHVP does not contain detectable traces of proteins or IgE-reactive peptides. This provides strong evidence that aHVP is very unlikely to trigger an allergic reaction to people who are intolerant or allergic to soy or wheat. [24] Earlier peer-reviewed animal studies done in 2006 also indicate that soy-hypersensitive dogs do not react to soy hydrolysate, a proposed protein source for soy-sensitive dogs. [25]

There are reports of a cosmetic-grade aHVP, Glupearl 19S (GP19S), inducing anaphylaxis when present in soap. Unlike food aHVP, this Japanese wheat aHVP is only very mildly hydrolyzed. [26] The unusual chemical condition makes GP19S more allergenic than pure gluten. [27] Newer regulations for cosmetic hydrolyzed wheat protein have been developed in response, requiring an average molecular mass of less than 3500 Da – about 35 residues long. In theory, "an allergen must have at least 2 IgE-binding epitopes, and each epitope must be at least 15 amino acid residues long, to trigger a type 1 hypersensitivity reaction." Experiments also show that this degree of hydrolysis is sufficient to not trigger IgE binding from GP19S-allergic patients. [26]

Allergenicity of eHVP depends on the specific food source and the enzyme used. Alcalase is able to render chickpea and green pea completely non-immunoreactive, where as papain only achieves partial reduction. Alcalase is also unable to make white beans non-reactive due to the antinutritional factors preventing complete digestion. [28] Alcalase, but not "Flavourzyme" (a commercial Aspergillus oryzae protease blend [29] for eHVP production), is able to make roasted peanut non-reactive. [30]

See also

Related Research Articles

<span class="mw-page-title-main">Miso</span> Traditional Japanese seasoning

Miso is a traditional Japanese seasoning. It is a thick paste produced by fermenting soybeans with salt and kōji and sometimes rice, barley, seaweed, or other ingredients. It is used for sauces and spreads, pickling vegetables, fish, or meats, and mixing with dashi soup stock to serve as miso soup, a Japanese culinary staple. Miso is high in protein and rich in vitamins and minerals, and it played an important nutritional role in feudal Japan. Miso is still widely used in both traditional and modern cooking in Japan and has been gaining worldwide interest.

<span class="mw-page-title-main">Trypsin</span> Family of digestive enzymes

Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin.

<span class="mw-page-title-main">Yeast extract</span> Cell contents of yeast without the cell walls, used as a food additive

Yeast extracts consist of the cell contents of yeast without the cell walls; they are used as food additives or flavorings, or as nutrients for bacterial culture media. They are often used to create savory flavors and umami taste sensations and can be found in a large variety of packaged food including frozen meals, crackers, snack foods, gravy, stock and more. They are rich in B vitamins. Yeast extracts and fermented foods contain glutamic acid, an amino acid which adds an umami flavor. Glutamic acid is found in meat, cheese, fungi and vegetables—such as broccoli and tomatoes. A number of other substances found in yeast extract provide aromas, some meat-like, when allowed to react under heat.

<span class="mw-page-title-main">Soy sauce</span> East Asian liquid condiment

Soy sauce is a liquid condiment of Chinese origin, traditionally made from a fermented paste of soybeans, roasted grain, brine, and Aspergillus oryzae or Aspergillus sojae molds. It is recognized for its pronounced umami taste.

<span class="mw-page-title-main">Monosodium glutamate</span> Chemical compound, flavor enhancer

Monosodium glutamate (MSG), also known as sodium glutamate, is a sodium salt of glutamic acid. MSG is found naturally in some foods including tomatoes and cheese in this glutamic acid form. MSG is used in cooking as a flavor enhancer with a savory taste that intensifies the meaty, savory flavor of food, as naturally occurring glutamate does in foods such as stews and meat soups.

<span class="mw-page-title-main">Maillard reaction</span> Chemical reaction that gives browned food flavor

The Maillard reaction is a chemical reaction between amino acids and reducing sugars to create melanoidins, the compounds which give browned food its distinctive flavor. Seared steaks, fried dumplings, cookies and other kinds of biscuits, breads, toasted marshmallows, and many other foods undergo this reaction. It is named after French chemist Louis Camille Maillard, who first described it in 1912 while attempting to reproduce biological protein synthesis. The reaction is a form of non-enzymatic browning which typically proceeds rapidly from around 140 to 165 °C. Many recipes call for an oven temperature high enough to ensure that a Maillard reaction occurs. At higher temperatures, caramelization and subsequently pyrolysis become more pronounced.

<span class="mw-page-title-main">Meat alternative</span> Plant-based food made to resemble meat

A meat alternative or meat substitute, is a food product made from vegetarian or vegan ingredients, eaten as a replacement for meat. Meat alternatives typically approximate qualities of specific types of meat, such as mouthfeel, flavor, appearance, or chemical characteristics. Plant- and fungus-based substitutes are frequently made with soy, but may also be made from wheat gluten as in seitan, pea protein as in the Beyond Burger, or mycoprotein as in Quorn. Alternative protein foods can also be made by precision fermentation, where single cell organisms such as yeast produce specific proteins using a carbon source; as well as cultivated or laboratory grown, based on tissue engineering techniques.

<span class="mw-page-title-main">Guanosine monophosphate</span> Chemical compound

Guanosine monophosphate (GMP), also known as 5′-guanidylic acid or guanylic acid, is a nucleotide that is used as a monomer in RNA. It is an ester of phosphoric acid with the nucleoside guanosine. GMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase guanine; hence it is a ribonucleotide monophosphate. Guanosine monophosphate is commercially produced by microbial fermentation.

Hydrolyzed protein is a solution derived from the hydrolysis of a protein into its component amino acids and peptides. While many means of achieving this exist, most common is prolonged heating with hydrochloric acid, sometimes with an enzyme such as pancreatic protease to simulate the naturally occurring hydrolytic process.

<span class="mw-page-title-main">Fermented bean curd</span> Chinese condiment

Fermented tofu is a Chinese condiment consisting of a form of processed, preserved tofu used in East Asian cuisine. The ingredients typically are soybeans, salt, rice wine and sesame oil or vinegar. In mainland China the product is often freshly distributed. In overseas Chinese communities living in Southeast Asia, commercially packaged versions are often sold in jars containing blocks 2- to 4-cm square by 1 to 2 cm thick soaked in brine with select flavorings.

<span class="mw-page-title-main">Soy allergy</span> Type of food allergy caused by soy

Soy allergy is a type of food allergy. It is a hypersensitivity to ingesting compounds in soy, causing an overreaction of the immune system, typically with physical symptoms, such as gastrointestinal discomfort, respiratory distress, or a skin reaction. Soy is among the eight most common foods inducing allergic reactions in children and adults. It has a prevalence of about 0.3% in the general population.

<span class="mw-page-title-main">Wheat allergy</span> Medical condition

Wheat allergy is an allergy to wheat which typically presents itself as a food allergy, but can also be a contact allergy resulting from occupational exposure. Like all allergies, wheat allergy involves immunoglobulin E and mast cell response. Typically the allergy is limited to the seed storage proteins of wheat. Some reactions are restricted to wheat proteins, while others can react across many varieties of seeds and other plant tissues. Wheat allergy is rare. Prevalence in adults was found to be 0.21% in a 2012 study in Japan.

<span class="mw-page-title-main">Glutamate flavoring</span> Generic name for flavor-enhancing compounds based on glutamic acid and its salts

Glutamate flavoring is the generic name for flavor-enhancing compounds based on glutamic acid and its salts (glutamates). These compounds provide an umami (savory) taste to food.

<span class="mw-page-title-main">3-MCPD</span> Chemical compound

3-MCPD (3-monochloropropane-1,2-diol or 3-chloropropane-1,2-diol) is an organic chemical compound with the formula HOCH2CH(OH)CH2Cl. It is a colorless liquid. It is a versatile multifunctional building block. The compound has attracted attention as the most common member of chemical food contaminants known as chloropropanols. It is suspected to be carcinogenic in humans.

Rice protein is a vegan protein isolate made from rice. It is often used as an alternative to the more common whey and soy protein isolates. To make it, brown rice is treated with enzymes that cause carbohydrates to separate from proteins. The resulting protein powder may then be flavored, and consumed with water, milk, or added to smoothies or health shakes.

Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain

Fish protein powder (FPP) describes a food grade powder product designated primarily for human consumption applications. It differs significantly from fish meal products which are designated for animal feed applications. Fish protein powders have various sanitary processing, purity and functional characteristics which establish them as human food ingredients. Production plants registered for the USA market are located in Peru and France.

<span class="mw-page-title-main">Hypoallergenic dog food</span>

Hypoallergenic dog food diets are created for dogs that experience food-related allergies causing adverse effects to their physical health.Super Hypoallergenic is enzymatic hydrolyzed hypoallergenic ostrich protein. The molecules that usually become allergens are intact proteins or glycoproteins. Hypoallergenic dog food diets offer a variety of protein sources that are unique by using proteins that are not recognized by the dog's antibodies as being antigens, minimizing allergic reactions for example Ostrich meat, bones and sinews. Adding novel protein sources, such as novel meats that a dog or its ancestors have never been exposed to is one method. Novel proteins can also be created by chemically modifying well known protein sources using hydrolysis techniques, rendering proteins unrecognizable by the gastrointestinal tract. Not all antigens are specific to proteins, however, and it is possible for anything that the body ingests to become an allergen. Providing diets with a limited amount of ingredients can be used for diagnostic purposes, as well as for dogs who are allergic to the common ingredients that are used in pet food. Certain nutrients are commonly incorporated into hypoallergenic dog food to help alleviate the symptoms of an allergic reaction. These ingredients include omega-3 fatty acids, Vitamins A and E, zinc, novel carbohydrates, and fiber.

<span class="mw-page-title-main">Corn sauce</span>

Corn sauce or fermented corn sauce is produced by fermentation using corn starch as the primary substrate. It is used as a food condiment and ingredient, both in paste and in powder form. Corn sauce, like soy sauce, has a characteristic savory taste. It is used to flavor dishes including soups, broths, and gravies.

References

  1. ↑ Manley/Fagerson (1971). Aspects of Aroma and Taste Characteristics of Hydrolysed Vegetable Protein, The Flavour Industry. p. 686 f.
  2. 1 2 3 Manley, C.H.; McCann, J.S.; Swaine, R.L. (1981), "The Chemical Bases of the Taste and Flavor Enhancing Properties of Hydrolyzed Protein", The Quality of Foods and Beverages, Elsevier, pp. 61–82, doi:10.1016/b978-0-12-169101-1.50011-2, ISBN   978-0-12-169101-1 , retrieved May 15, 2024
  3. ↑ "Würzen". Ullmanns Encyclopedia of Technical Chemistry. Vol. 18 (3rd ed.). Munich, Berlin, Vienna. 1967.{{cite book}}: CS1 maint: location missing publisher (link)
  4. ↑ Reineccius (1994). Source Book of Flavours. Springer. p. 140.
  5. ↑ Fischer, Research about amino acids, Springer 1906
  6. ↑ D. M. P. Phillips (1954). "Threonine and the Odour of Protein Hydrolysates". Nature. 173 (4414): 1092–1093. Bibcode:1954Natur.173.1092P. doi:10.1038/1731092a0. S2CID   4246025.
  7. 1 2 Prendergast (1974). "Protein Hydrolysate – A review". Food Trade Review: 14 f.
  8. ↑ Goesaert, Hans; Courtin, Christophe M.; Delcour, Jan A. (2008), "Use of enzymes in the production of cereal-based functional foods and food ingredients", Gluten-Free Cereal Products and Beverages, Elsevier, pp. 237–265, ISBN   978-0-12-373739-7 , retrieved May 14, 2024
  9. ↑ Aaslyng, Margit Dall; Martens, Magni; Poll, Leif; Nielsen, Per Munk; Flyge, Hanne; Larsen, Lone Melchior (February 1, 1998). "Chemical and Sensory Characterization of Hydrolyzed Vegetable Protein, a Savory Flavoring". Journal of Agricultural and Food Chemistry. 46 (2): 481–489. doi:10.1021/jf970556e. ISSN   0021-8561.
  10. ↑ Weir, G. S. D. (1992), "Proteins as a Source of Flavour", Biochemistry of Food Proteins, Boston, MA: Springer US, pp. 363–408, ISBN   978-1-4684-9897-4 , retrieved May 14, 2024
  11. 1 2 3 "Code of practice for the Reduction of 3-Monochlorpropanole-1,2-Diol (3-MCPD) during the Production of acid-HVPs and products that contain acid-HVPs CAC/RCP 64-2008" (PDF).
  12. ↑ Solms, Juerg (July 1969). "Taste of amino acids, peptides, and proteins". Journal of Agricultural and Food Chemistry (4): 686–688. doi:10.1021/jf60164a016. ISSN   0021-8561 . Retrieved May 15, 2024.
  13. ↑ Nissen, Steven (1992), "Amino Acid Analysis in Food and in Physiological Samples", Modern Methods in Protein Nutrition and Metabolism, Elsevier, pp. 1–8, ISBN   978-0-12-519570-6 , retrieved May 15, 2024
  14. ↑ Finley, John W.; Hopkins, Daniel T.; American Association of Cereal Chemists, eds. (1985). Digestibility and amino acid availability in cereals and oilseeds. St. Paul, Minn: American Association of Cereal Chemists. ISBN   978-0-913250-40-2.
  15. ↑ Hurrell, R. F.; Carpenter, K. J. (1981). "The estimation of available lysine foodstuffs after Maillard reactions". Progress in Food & Nutrition Science. 5 (1–6): 159–176. ISSN   0306-0632. PMID   6798628.
  16. ↑ Mauron, J.; Mottu, F.; Bujard, E.; Egli, R.H. (1955). "The availability of lysine, methionine and tryptophan in condensed milk and milk powder. In vitro digestion studies". Archives of Biochemistry and Biophysics. 59 (2): 433–451. doi:10.1016/0003-9861(55)90510-5.
  17. ↑ Finot, P. A.; Bricout, J.; Viani, R.; Mauron, J. (1968). "Identification of a new lysine derivative obtained upon acid hydrolysis of heated milk". Experientia. 24 (11): 1097–1099. doi:10.1007/BF02147778. ISSN   0014-4754.
  18. 1 2 3 4 Kale, Prajyoti; Mishra, Anusha; Annapure, Uday S. (June 2022). "Development of vegan meat flavour: A review on sources and techniques". Future Foods. 5: 100149. doi: 10.1016/j.fufo.2022.100149 . S2CID   248838839.
  19. ↑ Wu, Yi-Fang G.; Cadwallader, Keith R. (May 8, 2002). "Characterization of the Aroma of a Meatlike Process Flavoring from Soybean-Based Enzyme-Hydrolyzed Vegetable Protein". Journal of Agricultural and Food Chemistry. 50 (10): 2900–2907. doi:10.1021/jf0114076. PMID   11982417.
  20. ↑ Jarunrattanasri, Arporn; Theerakulkait, Chockchai; Cadwallader, Keith R. (April 1, 2007). "Aroma Components of Acid-Hydrolyzed Vegetable Protein Made by Partial Hydrolysis of Rice Bran Protein". Journal of Agricultural and Food Chemistry. 55 (8): 3044–3050. doi:10.1021/jf0631474. PMID   17367160.
  21. ↑ Blank, Imre; Schieberle, Peter (July 1993). "Analysis of the seasoning-like flavour substances of a commercial lovage extract (Levisticum officinale Koch.)". Flavour and Fragrance Journal. 8 (4): 191–195. doi:10.1002/ffj.2730080405.
  22. ↑ Li, Xuejie; Li, Jian (2020). "The Flavor of Plant-Based Meat Analogues". Cereal Foods World. 65 (4). doi:10.1094/CFW-65-4-0040. S2CID   231203281.
  23. ↑ "Code of practice for Bouillons and Consommés".
  24. ↑ Reuter A, Gerald R, Kuehne Y, Engin A, Przywara J, Worm M, Ballmer-Weber B, Holzhauser T, Vieths S. Evaluation of the allergenic potential of soy and wheat based seasonings. XXIX EAACI Congress of the European Academy of Allergy and Clinical Immunology. p. 322. doi:10.1111/j.1398-9995.2010.02393.x. PMC   7159487 .
  25. ↑ Puigdemont, A; Brazís, P; Serra, M; Fondati, A (March 2006). "Immunologic responses against hydrolyzed soy protein in dogs with experimentally induced soy hypersensitivity". American Journal of Veterinary Research. 67 (3): 484–8. doi: 10.2460/ajvr.67.3.484 . PMID   16506912.
  26. 1 2 Burnett, Christina; Bergfeld, Wilma F.; Belsito, Donald V.; Hill, Ronald A.; Klaassen, Curtis D.; Liebler, Daniel C.; Marks, James G.; Shank, Ronald C.; Slaga, Thomas J.; Snyder, Paul W.; Andersen, F. Alan; Heldreth, Bart (May 2018). "Safety Assessment of Hydrolyzed Wheat Protein and Hydrolyzed Wheat Gluten as Used in Cosmetics". International Journal of Toxicology. 37 (1_suppl): 55S–66S. doi: 10.1177/1091581818776013 . PMID   29761728. S2CID   46889452.
  27. ↑ Nakamura, Masashi; Yagami, Akiko; Hara, Kazuhiro; Sano, Akiyo; Kobayashi, Tsukane; Matsunaga, Kayoko (February 2015). "Antigens in Glupearl 19S Were Developed By Acid-Heat Treatment". Journal of Allergy and Clinical Immunology. 135 (2): AB254. doi:10.1016/j.jaci.2014.12.1771.
  28. ↑ Calcinai, Luisa; Bonomini, Maria Giulia; Leni, Giulia; Faccini, Andrea; Puxeddu, Ilaria; Giannini, Daiana; Petrelli, Fiorella; Prandi, Barbara; Sforza, Stefano; Tedeschi, Tullia (October 7, 2022). "Effectiveness of enzymatic hydrolysis for reducing the allergenic potential of legume by-products". Scientific Reports. 12 (1): 16902. Bibcode:2022NatSR..1216902C. doi:10.1038/s41598-022-21296-z. hdl: 10807/230858 . PMC   9547019 . PMID   36207409.
  29. ↑ Merz, Michael; Eisele, Thomas; Berends, Pieter; Appel, Daniel; Rabe, Swen; Blank, Imre; Stressler, Timo; Fischer, Lutz (June 17, 2015). "Flavourzyme, an Enzyme Preparation with Industrial Relevance: Automated Nine-Step Purification and Partial Characterization of Eight Enzymes". Journal of Agricultural and Food Chemistry. 63 (23): 5682–5693. doi:10.1021/acs.jafc.5b01665. PMID   25996918.
  30. ↑ Cabanillas, Beatriz; Pedrosa, Mercedes M.; Rodríguez, Julia; Muzquiz, Mercedes; Maleki, Soheila J.; Cuadrado, Carmen; Burbano, Carmen; Crespo, Jesús F. (2012). "Influence of Enzymatic Hydrolysis on the Allergenicity of Roasted Peanut Protein Extract". International Archives of Allergy and Immunology. 157 (1): 41–50. doi:10.1159/000324681. PMID   21912172. S2CID   25496670.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.