NL2029200A - Gluten-free hypoallergenic soy protein flour and preparation method thereof - Google Patents
Gluten-free hypoallergenic soy protein flour and preparation method thereof Download PDFInfo
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- NL2029200A NL2029200A NL2029200A NL2029200A NL2029200A NL 2029200 A NL2029200 A NL 2029200A NL 2029200 A NL2029200 A NL 2029200A NL 2029200 A NL2029200 A NL 2029200A NL 2029200 A NL2029200 A NL 2029200A
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- soy protein
- solution
- hypoallergenic
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- polyphenols
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- 229940001941 soy protein Drugs 0.000 title claims abstract description 96
- 108010073771 Soybean Proteins Proteins 0.000 title claims abstract description 90
- 235000013312 flour Nutrition 0.000 title claims abstract description 53
- 230000000774 hypoallergenic effect Effects 0.000 title claims abstract description 53
- 238000002360 preparation method Methods 0.000 title claims abstract description 20
- 239000000243 solution Substances 0.000 claims abstract description 65
- 150000008442 polyphenolic compounds Chemical class 0.000 claims abstract description 24
- 235000013824 polyphenols Nutrition 0.000 claims abstract description 24
- 239000000843 powder Substances 0.000 claims abstract description 22
- 229920001542 oligosaccharide Polymers 0.000 claims abstract description 18
- 150000002482 oligosaccharides Polymers 0.000 claims abstract description 18
- 239000000376 reactant Substances 0.000 claims abstract description 16
- 150000004676 glycans Chemical class 0.000 claims abstract description 15
- 229920001282 polysaccharide Polymers 0.000 claims abstract description 15
- 239000005017 polysaccharide Substances 0.000 claims abstract description 15
- 238000000034 method Methods 0.000 claims abstract description 11
- 238000004108 freeze drying Methods 0.000 claims abstract description 7
- 235000013305 food Nutrition 0.000 claims description 11
- 229940074393 chlorogenic acid Drugs 0.000 claims description 8
- 229950001002 cianidanol Drugs 0.000 claims description 8
- 229940016667 resveratrol Drugs 0.000 claims description 8
- 229940071440 soy protein isolate Drugs 0.000 claims description 7
- PFTAWBLQPZVEMU-DZGCQCFKSA-N (+)-catechin Chemical compound C1([C@H]2OC3=CC(O)=CC(O)=C3C[C@@H]2O)=CC=C(O)C(O)=C1 PFTAWBLQPZVEMU-DZGCQCFKSA-N 0.000 claims description 6
- CWVRJTMFETXNAD-FWCWNIRPSA-N 3-O-Caffeoylquinic acid Natural products O[C@H]1[C@@H](O)C[C@@](O)(C(O)=O)C[C@H]1OC(=O)\C=C\C1=CC=C(O)C(O)=C1 CWVRJTMFETXNAD-FWCWNIRPSA-N 0.000 claims description 6
- PZIRUHCJZBGLDY-UHFFFAOYSA-N Caffeoylquinic acid Natural products CC(CCC(=O)C(C)C1C(=O)CC2C3CC(O)C4CC(O)CCC4(C)C3CCC12C)C(=O)O PZIRUHCJZBGLDY-UHFFFAOYSA-N 0.000 claims description 6
- 229920001503 Glucan Polymers 0.000 claims description 6
- CWVRJTMFETXNAD-KLZCAUPSSA-N Neochlorogenin-saeure Natural products O[C@H]1C[C@@](O)(C[C@@H](OC(=O)C=Cc2ccc(O)c(O)c2)[C@@H]1O)C(=O)O CWVRJTMFETXNAD-KLZCAUPSSA-N 0.000 claims description 6
- QNVSXXGDAPORNA-UHFFFAOYSA-N Resveratrol Natural products OC1=CC=CC(C=CC=2C=C(O)C(O)=CC=2)=C1 QNVSXXGDAPORNA-UHFFFAOYSA-N 0.000 claims description 6
- LUKBXSAWLPMMSZ-OWOJBTEDSA-N Trans-resveratrol Chemical compound C1=CC(O)=CC=C1\C=C\C1=CC(O)=CC(O)=C1 LUKBXSAWLPMMSZ-OWOJBTEDSA-N 0.000 claims description 6
- ADRVNXBAWSRFAJ-UHFFFAOYSA-N catechin Natural products OC1Cc2cc(O)cc(O)c2OC1c3ccc(O)c(O)c3 ADRVNXBAWSRFAJ-UHFFFAOYSA-N 0.000 claims description 6
- 235000005487 catechin Nutrition 0.000 claims description 6
- CWVRJTMFETXNAD-JUHZACGLSA-N chlorogenic acid Chemical compound O[C@@H]1[C@H](O)C[C@@](O)(C(O)=O)C[C@H]1OC(=O)\C=C\C1=CC=C(O)C(O)=C1 CWVRJTMFETXNAD-JUHZACGLSA-N 0.000 claims description 6
- 235000001368 chlorogenic acid Nutrition 0.000 claims description 6
- FFQSDFBBSXGVKF-KHSQJDLVSA-N chlorogenic acid Natural products O[C@@H]1C[C@](O)(C[C@@H](CC(=O)C=Cc2ccc(O)c(O)c2)[C@@H]1O)C(=O)O FFQSDFBBSXGVKF-KHSQJDLVSA-N 0.000 claims description 6
- BMRSEYFENKXDIS-KLZCAUPSSA-N cis-3-O-p-coumaroylquinic acid Natural products O[C@H]1C[C@@](O)(C[C@@H](OC(=O)C=Cc2ccc(O)cc2)[C@@H]1O)C(=O)O BMRSEYFENKXDIS-KLZCAUPSSA-N 0.000 claims description 6
- 235000021255 galacto-oligosaccharides Nutrition 0.000 claims description 6
- 150000003271 galactooligosaccharides Chemical class 0.000 claims description 6
- 235000021283 resveratrol Nutrition 0.000 claims description 6
- XFZJEEAOWLFHDH-UHFFFAOYSA-N (2R,2'R,3R,3'R,4R)-3,3',4',5,7-Pentahydroxyflavan(48)-3,3',4',5,7-pentahydroxyflavan Natural products C=12OC(C=3C=C(O)C(O)=CC=3)C(O)CC2=C(O)C=C(O)C=1C(C1=C(O)C=C(O)C=C1O1)C(O)C1C1=CC=C(O)C(O)=C1 XFZJEEAOWLFHDH-UHFFFAOYSA-N 0.000 claims description 4
- KSEBMYQBYZTDHS-HWKANZROSA-M (E)-Ferulic acid Natural products COC1=CC(\C=C\C([O-])=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-M 0.000 claims description 4
- CWEZAWNPTYBADX-UHFFFAOYSA-N Procyanidin Natural products OC1C(OC2C(O)C(Oc3c2c(O)cc(O)c3C4C(O)C(Oc5cc(O)cc(O)c45)c6ccc(O)c(O)c6)c7ccc(O)c(O)c7)c8c(O)cc(O)cc8OC1c9ccc(O)c(O)c9 CWEZAWNPTYBADX-UHFFFAOYSA-N 0.000 claims description 4
- MOJZMWJRUKIQGL-FWCKPOPSSA-N Procyanidin C2 Natural products O[C@@H]1[C@@H](c2cc(O)c(O)cc2)Oc2c([C@H]3[C@H](O)[C@@H](c4cc(O)c(O)cc4)Oc4c3c(O)cc(O)c4)c(O)cc(O)c2[C@@H]1c1c(O)cc(O)c2c1O[C@@H]([C@H](O)C2)c1cc(O)c(O)cc1 MOJZMWJRUKIQGL-FWCKPOPSSA-N 0.000 claims description 4
- KSEBMYQBYZTDHS-HWKANZROSA-N ferulic acid Chemical compound COC1=CC(\C=C\C(O)=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-N 0.000 claims description 4
- 235000001785 ferulic acid Nutrition 0.000 claims description 4
- 229940114124 ferulic acid Drugs 0.000 claims description 4
- KSEBMYQBYZTDHS-UHFFFAOYSA-N ferulic acid Natural products COC1=CC(C=CC(O)=O)=CC=C1O KSEBMYQBYZTDHS-UHFFFAOYSA-N 0.000 claims description 4
- HGVVOUNEGQIPMS-UHFFFAOYSA-N procyanidin Chemical compound O1C2=CC(O)=CC(O)=C2C(O)C(O)C1(C=1C=C(O)C(O)=CC=1)OC1CC2=C(O)C=C(O)C=C2OC1C1=CC=C(O)C(O)=C1 HGVVOUNEGQIPMS-UHFFFAOYSA-N 0.000 claims description 4
- 229920002414 procyanidin Polymers 0.000 claims description 4
- 238000003756 stirring Methods 0.000 claims description 4
- QURCVMIEKCOAJU-UHFFFAOYSA-N trans-isoferulic acid Natural products COC1=CC=C(C=CC(O)=O)C=C1O QURCVMIEKCOAJU-UHFFFAOYSA-N 0.000 claims description 4
- 101710102211 11S globulin Proteins 0.000 claims description 3
- 101000767750 Carya illinoinensis Vicilin Car i 2.0101 Proteins 0.000 claims description 3
- 101000767759 Corylus avellana Vicilin Cor a 11.0101 Proteins 0.000 claims description 3
- 101710190853 Cruciferin Proteins 0.000 claims description 3
- 101000622316 Juglans regia Vicilin Jug r 2.0101 Proteins 0.000 claims description 3
- 101000767757 Pinus koraiensis Vicilin Pin k 2.0101 Proteins 0.000 claims description 3
- 101000767758 Pistacia vera Vicilin Pis v 3.0101 Proteins 0.000 claims description 3
- 239000012141 concentrate Substances 0.000 claims description 3
- 235000005911 diet Nutrition 0.000 claims description 3
- 230000000378 dietary effect Effects 0.000 claims description 3
- 238000007710 freezing Methods 0.000 claims description 3
- 230000008014 freezing Effects 0.000 claims description 3
- 150000003272 mannan oligosaccharides Chemical class 0.000 claims description 3
- 230000001105 regulatory effect Effects 0.000 claims description 2
- 235000012054 meals Nutrition 0.000 claims 6
- 238000002156 mixing Methods 0.000 claims 1
- 239000012460 protein solution Substances 0.000 claims 1
- 239000007864 aqueous solution Substances 0.000 abstract description 3
- 150000001720 carbohydrates Chemical class 0.000 description 22
- 108010005094 Advanced Glycation End Products Proteins 0.000 description 20
- 230000000052 comparative effect Effects 0.000 description 16
- RRUYWEMUWIRRNB-LURJTMIESA-N (2s)-6-amino-2-[carboxy(methyl)amino]hexanoic acid Chemical compound OC(=O)N(C)[C@H](C(O)=O)CCCCN RRUYWEMUWIRRNB-LURJTMIESA-N 0.000 description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 239000000047 product Substances 0.000 description 12
- 235000010469 Glycine max Nutrition 0.000 description 10
- 235000018102 proteins Nutrition 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 230000036252 glycation Effects 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 description 6
- 229920001661 Chitosan Polymers 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 239000013566 allergen Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 244000068988 Glycine max Species 0.000 description 4
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- 239000012153 distilled water Substances 0.000 description 4
- 230000036571 hydration Effects 0.000 description 4
- 238000006703 hydration reaction Methods 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
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- 235000017807 phytochemicals Nutrition 0.000 description 2
- 229930000223 plant secondary metabolite Natural products 0.000 description 2
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- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- 208000018522 Gastrointestinal disease Diseases 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
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- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
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- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
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- 150000008163 sugars Chemical class 0.000 description 1
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- 238000005406 washing Methods 0.000 description 1
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
- A23J3/14—Vegetable proteins
- A23J3/16—Vegetable proteins from soybean
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/045—Hydroxy compounds, e.g. alcohols; Salts thereof, e.g. alcoholates
- A61K31/05—Phenols
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/192—Carboxylic acids, e.g. valproic acid having aromatic groups, e.g. sulindac, 2-aryl-propionic acids, ethacrynic acid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/21—Esters, e.g. nitroglycerine, selenocyanates
- A61K31/215—Esters, e.g. nitroglycerine, selenocyanates of carboxylic acids
- A61K31/216—Esters, e.g. nitroglycerine, selenocyanates of carboxylic acids of acids having aromatic rings, e.g. benactizyne, clofibrate
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/335—Heterocyclic compounds having oxygen as the only ring hetero atom, e.g. fungichromin
- A61K31/35—Heterocyclic compounds having oxygen as the only ring hetero atom, e.g. fungichromin having six-membered rings with one oxygen as the only ring hetero atom
- A61K31/352—Heterocyclic compounds having oxygen as the only ring hetero atom, e.g. fungichromin having six-membered rings with one oxygen as the only ring hetero atom condensed with carbocyclic rings, e.g. methantheline
- A61K31/353—3,4-Dihydrobenzopyrans, e.g. chroman, catechin
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/105—Plant extracts, their artificial duplicates or their derivatives
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/185—Vegetable 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/20—Reducing nutritive value; Dietetic products with reduced nutritive value
- A23L33/21—Addition of substantially indigestible substances, e.g. dietary fibres
-
- 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
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- Health & Medical Sciences (AREA)
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- Medicinal Chemistry (AREA)
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- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Nutrition Science (AREA)
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- Organic Chemistry (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Emergency Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The present invention relates to gluten-free hypoallergenic soy protein flour and a preparation method thereof. The method comprises: adding indicated polyphenols into a soy protein aqueous solution, well agitating the solution, adjusting the pH value of the solution to be alkaline, and allowing the solution to react in the dark at room temperature for 24 h to obtain a polyphenol-soy protein covalent compleX solution, adding oligo/polysaccharides into the polyphenol-soy protein covalent compleX solution, and well agitating the solution to obtain a reacting solution, freeze-drying the reacting solution to obtain reactant powder, and allowing the reactant powder to react for 12-36 h at 55-65 ° C at a relative humidity of 75% to obtain the hypoallergenic soy protein flour.
Description
METHOD THEREOF Technical Field
[0001] The present invention relates to the field of food processing, specifically to hypoallergenic soy protein flour and a preparation method thereof. Background
[0002] Soy proteins feature a high nutritional value, easy preparation, broad sources, low cost, etc. As one of a few types of plant proteins that can replace animal proteins, soy proteins have become one of the most important raw materials in the food industry. However, soybean is listed among the “big eight” food allergens as recognized by the Food and Agriculture Organization of the United Nations. Currently, about 0.27%-1.9% of the adult population and 0.4% of the infants and children are allergic to soybeans, with clinical symptoms of nasitis, erythra, asthma, gastrointestinal disorders, etc. In serious cases, the healthy growth and physiological development of the infants and children can be detrimentally affected. Nowadays, along with the development of the food industry and processing technology, applications of soy proteins in related fields would keep expanding, and the incidence of soybean allergy is likely to grow up. Considering this, mitigation of the allergenicity of soy proteins is of crucial and realistic significance with a broad market prospect in the food industry.
[0003] Glycation is an effective approach that has been used to reduce the allergenicity of soy proteins. Its principle is to use the non-enzymatic browning reaction (Maillard reaction) occurred between reducing sugars and proteins to induce cross-linking and side-chain branching among polypeptide chains. Following glycation, the protein conformational structures were modified and the related allergen epitopes were mapped or damaged at various degrees, thus obtaining hypoallergenic soy protein products. During protein glycoxidation, a series of undesired Maillard reaction products can be generated. In particular, the advanced glycation end-products (AGEs) are a group of heterogeneous molecules formed in the “advanced” stage of protein glycation, and have been associated with the pathogenesis of various progressive diseases, such as type-2 diabetes, chronic kidney disorders, and cardiovascular diseases. In this scenario, as it is relatively difficult to control the glycative reactions, this brings potential pitfalls for the application of saccharide modified hypoallergenic protein products.
[0004] The present invention is aimed to solve one of technical problems in relevant art to a certain extent. For this reason, an objective of the present invention is to provide a preparation method of hypoallergenic soy protein flour. The method can minimize the content of AGEs while maintaining reduction in the products’ low allergenicity, thus avoiding adverse effects of the glycation side products on human body.
[0005] For this reason, on the one hand, the present invention provides a preparation method of hypoallergenic soy protein flour, including the following steps:
[0006] Adding dietary polyphenols into a soy protein aqueous solution. After vigorous stirring, the pH of the solution was adjusted to be alkaline, and the mixture was incubated in the dark at room temperature for 24 h to obtain a polyphenol-soy protein covalent complex solution;
[0007] Adding indicated oligo/polysaccharides into the polyphenol-soy protein covalent complex solution. Stirring the mixture well to obtain a reacting solution;
[0008] Freeze-drying the reacting solution to obtain reactant powder;
[0009] Allowing the reactant powder to react at 55-65 °C for 12-36 h at a relative humidity of 75% to obtain the hypoallergenic soy protein flour.
[0010] According to the preparation method of the hypoallergenic soy protein flour in an embodiment of the present invention, the added polyphenols can form covalent complexes with proteins through autooxidation under alkaline conditions, inducing changes in the conformational structures and physicochemical characteristics of the reacted proteins. Of note, the obtained polyphenol-allergenic protein complex has relatively high resistance to glycoxidation with potentially low allergenicity. Combining covalent complexation and dry-heat glycation would induce cross-linking and side-chain branching among polypeptide chains to damage the epitopes of soy protein allergens. In the meantime, ascribed to the anti-oxidant power of polyphenols and their quinone intermediates, along with the steric-hindrance effect of the oligo/polysaccharides, the obtained final products features low levels of AGEs with diminished allergenicity and desired functional properties, thus avoiding the adverse effects of AGEs on the human body. The present method is convenient and easily operated with an additional improvement effect, and the prepared soy protein flour features good flavors and safety, which can be readily commercialized the food industry.
[0011] In addition, the preparation method of hypoallergenic soy protein flour provided by the previously described embodiment of the present invention also includes the following additional technical characteristics:
[0012] Optionally, the pH value of the solution is regulated to 9.0.
[0013] Optionally, the soy proteins are any of the followings: soy protein concentrate, soy protein isolate, 7S globulin and 11S globulin.
[0014] Optionally, the indicated polyphenols are any of the followings, or a combination of them or a botanical extract rich in those phytochemicals: chlorogenic acid, ferulic acid, resveratrol, catechin and procyanidin.
[0015] Optionally, the oligo/polysaccharides are any of the followings or a combination of them: galacto-oligosaccharide, mannan oligosaccharide, oligochitosan and glucan.
[0016] Optionally, the added dietary polyphenols are 25-100 umol/’g soy proteins.
[0017] Optionally, the mass ratio of the oligosaccharides to soy proteins is 1:1-4:1.
[0018] Optionally, the freeze-drying is performed by 24-h pre-freezing at -20 °C prior to 16-24 h freeze-drying at -40~-50 °C.
[0019] On the other hand, the present invention provides hypoallergenic soy protein flour, prepared by the previously described preparation method of hypoallergenic soy protein flour.
[0020] According to the hypoallergenic soy protein flour of the present invention, hypoallergenic soy protein flour with minimized AGEs can be prepared by the previously described method.
[0021] The additional characteristics and advantages of the present invention will be partly described below, and some will become apparent from the following description or be perceived through implementation of the present invention.
[0022] FIG. 1 illustrates the content of fluorescent AGEs in hypoallergenic soy protein flour according to an embodiment of the present invention,
[0023] FIG. 2 illustrates the content of CML in hypoallergenic soy protein flour according to an embodiment of the present invention;
[0024] FIG. 3 illustrates the IgE-binding ability of hypoallergenic soy protein flour according to an embodiment of the present invention.
[0025] The following describes the technical solutions of the present invention through specific embodiments. It should be understood that, one or more steps mentioned in the present invention do not exclude other steps prior to or behind the sequenced steps or other steps inserted among those clearly mentioned steps. It should also be understood that, those embodiments are used to merely describe the present invention, not to limit the scope of the present invention. Moreover, unless otherwise specified, the serial numbers of steps are only convenient tools for distinguishing the steps instead of limiting the sequence of the steps or limiting the implementable scope of the present invention. Change or adjustment of the relative relationship of the serial numbers should also be deemed to fall within the implementable scope of the present invention if there is no substantial change to the technical contents.
[0026] To facilitate a better understanding of the previously described technical solution, exemplary embodiments of the present invention will be described in further detail.
Although exemplary embodiments of the present invention are illustrated, it should be understood that the present invention can be implemented in various forms and should not be limited by embodiments described herein. On the contrary, those embodiments are provided to help more thoroughly understand the present invention and entirely pass on the scope of the present invention to those skilled in the art.
[0027] All test materials used in the present invention are common products commercially available at the market.
[0028] In the present invention, the room temperature is 25 °C.
[0029] An embodiment of the present invention provides a preparation method of hypoallergenic soy protein flour, including the following steps (optimum conditions):
[0030] (1) Indicated polyphenols are added to a soy protein aqueous solution; the solution is vigorously stirred; the pH of the solution is adjusted to be alkaline; and the mixture was allowed to react in the dark at room temperature for 24 h to obtain a polyphenol-soy protein covalent complex solution. According to a specific embodiment of the present invention, soy proteins can be dispersed in distilled water to a final concentration of 50 mg/mL; then, 25-100 umol/g protein of indicated polyphenols are added; the solution is well agitated for complete hydration; 2 mol/L NaOH is added to adjust the pH of the solution to 9.0; and the solution 1s kept under atmospheric air at room temperature in the dark for 24 h to obtain a covalent complex solution. The indicated polyphenols can be any of the followings, or a combination of them or a botanical extract rich in those phytochemicals: chlorogenic acid, ferulic acid, resveratrol, catechin and procyanidin. The soy proteins can be any one of soy protein concentrate, soy protein isolate, 7S globulin and 11S globulin.
[0031] (2) Oligo/polysaccharides are added into the polyphenol-soy protein covalent product solution, and the solution is well agitated to obtain a reacting solution. According to a specific embodiment of the present invention, the covalent product solution can be added with oligochitosan in an amount of 4 times of the mass of soy protein isolate flour. The oligo/polysaccharides can be any one of the followings or a combination of them: galacto-oligosaccharide, mannan oligosaccharide, oligochitosan and glucan.
[0032] (3) The obtained reacting solution is frozen at -20°C, and then lyophilized to 5 obtain reactant powder. According to a specific embodiment of the present invention, the reacting solution can be immediately stored in a -20 °C refrigerator, and after 24-h pre-freezing, the solution was freeze-dried at -40 °C~-50 °C for 16-24 h to obtain the reactant powder.
[0033] (4) The reactant powder was allowed to react at 55 °C-65 °C for 12-36 h at a relative humidity of 75% to obtain the hypoallergenic soy protein flour. According to a specific embodiment of the present invention, the reactant powder can be dry-heated at 60 °C for 36 h at a 75% humidity.
[0034] Therefore, combining covalent complexation with dry-heat glycation can damage the epitopes of soy protein allergens; meanwhile, the anti-oxidant powers of the polyphenols and their quinone intermediates, along with the steric-hindrance effect of the oligo/polysaccharides specifically reduced the formation of AGEs in the products, such that the obtained flour features low AGEs level and desired hypo-allergenicity. The IgE-binding ability of the hypoallergenic soy protein flour prepared by the present method is reduced by
45.7%-61.3%, compared to the native control; at the same time, the content of the fluorescent AGEs was decreased by 58.9%-70.3%, and the levels of carboxy methyl lysine (CML) was diminished by 39.7%-50.5%, in comparison to the polyphenol-absent group. This method features convenience, easy operation, and high product quality and safety, which can be readily commercialized the food industry.
[0035] The followings describe the present invention by reference to specific embodiments. It should be noted that those embodiments are merely descriptive and do not limit the present invention in any way.
[0036] Embodiment 1
[0037] (1) 5000 mg of soy protein isolate flour and 1772 mg of chlorogenic acid (equivalent to 100 umol/g soy proteins) were added into 100 mL of distilled water; the mixture was stirred for 2 h at room temperature for complete hydration; then, 2 mol/L NaOH was added to adjust the pH value to 9.0; next, the solution was exposed under atmospheric air at room temperature in the dark for 24 h to obtain a soy protein-chlorogenic acid covalent complex solution.
[0038] (2) 20000 mg of oligochitosan were added to the soy protein-chlorogenic acid covalent complex solution obtained in step (1), where the mass ratio of the soy proteins to the oligochitosan was 1:4; the solution was constantly stirred for 30 min to obtain a reacting solution.
[0039] (3) The reacting solution obtained in step (2) was stored in a -20 °C refrigerator and pre-frozen for 24 h, then freeze-dried at -45 °C for 24 h to obtain reactant powder.
[0040] (4) The reactant powder obtained in step (3) was allowed to react for at 60 °C 36 h at 75% humidity to obtain saccharide modified solid powder.
[0041] (5) The saccharide modified solid powder obtained in step (4) was ground and sieved using a 100-mesh screen to obtain the hypoallergenic soy protein flour.
[0042] Embodiment 2
[0043] (2) 5000 mg of soy protein isolate flour and 36 mg of catechin (equivalent to 25 umol/g soy proteins) were added into 100 mL of distilled water; the mixture was stirred for 2 h at room temperature for complete hydration; then, 2 mol/L NaOH was added to adjust the pH value of the solution to 9.0; next, the solution was exposed under atmospheric air at room temperature in the dark for 24 h to obtain a soy protein-catechin covalent complex solution.
[0044] (2) 5000 mg of galacto-oligosaccharides were added into the soy protein-catechin covalent complex solution obtained in step (1), where the mass ratio of the soy proteins to the galactooligosaccharides was 1:1; and, the solution was constantly stirred for 30 min to obtain a reacting solution.
[0045] (3) The reacting solution obtained in step (2) was stored in a -20 °C refrigerator and pre-frozen for 24 h, then freeze-dried at -45 °C for 24 h to obtain reactant powder.
[0046] (4) The reactant powder obtained in step (3) was allowed to react for 12 h at 55 °C at 75% humidity to obtain saccharide modified solid powder.
[0047] (5) The saccharide modified solid powder obtained in step (4) was ground and sieved using a 100-mesh screen to obtain the hypoallergenic soy protein flour.
[0048] Embodiment 3
[0049] (1) 5000 mg of soy protein isolate flour and 57 mg of resveratrol (equivalent to 50 umol/g soy proteins) were added into 100 mL of distilled water; the mixture solution was stirred for 2 h at room temperature for complete hydration; then, 2 mol/L NaOH was added to adjust the pH value of the solution to 9.0; next, the solution was exposed under atmospheric air at room temperature in the dark for 24 h to obtain a soy protein-resveratrol covalent complex solution.
[0050] (2) 10000 mg of glucans (with a molecular weight of 10 kDa) were added into the soy protein-resveratrol covalent complex solution obtained in step (1), where the mass ratio of the soy proteins to the glucans was 1:2; and, the solution was constantly stirred for 30 min to obtain a reacting solution.
[0051] (3) The reacting solution obtained in step (2) was stored in a -20 °C refrigerator and pre-frozen for 24 h, then freeze-dried at -45 °C for 24 h to obtain reactant powder.
[0052] (4) The reactant powder obtained in step (3) was reacted for 24 h at 65 °C at 75% humidity to obtain saccharide modified solid powder.
[0053] (5) The saccharide modified solid powder obtained in step (4) was ground and sieved using a 100-mesh screen to obtain the hypoallergenic soy protein flour.
[0054] Comparative example 1
[0055] Comparative example 1 is different from the embodiment 1 in that, the oligochitosan were replaced by glucose, and chlorogenic acid was not used. The others were identical with those in the embodiment 1.
[0056] Comparative example 2
[0057] Comparative example 2 is different from the embodiment 2 in that, galacto-oligosaccharides were replaced by fructose, and catechin was not used. The others were identical with those in the embodiment 1.
[0058] Comparative example 3
[0059] Comparative example 3 is different from the embodiment 3 in that, glucans were replaced by ribose, and resveratrol was not used. The others were identical with those in the embodiment 3.
[0060] Experimental examples
[0061] The hypoallergenic soy protein flour prepared in embodiments 1-3 and that prepared in comparative examples 1-3 was used as test samples to test the properties of the glycated soy protein product.
[0062] 1. Analysis of fluorescent AGEs formation
[0063] A tested sample solution with a concentration of 5 mg/mL was measured in a fluorospectrophotometer. The excitation wavelength was 350 nm and the emission wavelength was 440 nm.
[0064] The AGEs content (%) = Fsampte/Fcontot * 100%. In this expression, the Fsampte and Foro: respectively represent the fluorescence intensity of the sample group (including oligo/polysaccharides and polyphenols) and the control group (including oligo/polysaccharides but polyphenols excluded).
[0065] The results can be seen in FIG. 1. The content of the fluorescent AGEs in the saccharide modified hypoallergenic soy protein flour in embodiments 1-3 is obviously lower that in the corresponding comparative examples. The content of the fluorescent AGEs in the saccharide modified hypoallergenic soy protein flour in embodiment 1 is 29.7% of that in the corresponding comparative example. The content of the fluorescent AGEs in the saccharide modified hypoallergenic soy protein flour in embodiment 2 is 41.1% of that in the corresponding comparative example. The content of the fluorescent AGEs in the saccharide modified hypoallergenic soy protein flour in embodiment 3 is 31.6% of that in the corresponding comparative example.
[0066] 2. Measurement of CML content
[0067] Commercially available CML ELISA kits were used to test the CML content in saccharide modified hypoallergenic soy protein flour solutions obtained in embodiments 1-3 and comparative examples 1-3.
[0068] CML content (%) = Csample/Ceonrot * 100%. In this expression, Csampte and Ceontrot respectively represent the CML content of the sample group (including oligo/polysaccharides and polyphenols) and the control group (including oligo/polysaccharides but polyphenols excluded).
[0069] The results can be seen in FIG. 1. The CML content of the saccharide modified hypoallergenic soy protein flour solution in embodiments 1-3 is obviously lower that in the corresponding comparative examples. The CML content of the saccharide modified hypoallergenic soy protein flour solution in embodiment 1 is 49.5% of that in the corresponding comparative example. The CML content of the saccharide modified hypoallergenic soy protein flour solution in embodiment 2 is 60.3% of that in the corresponding comparative example. The CML content of the saccharide modified hypoallergenic soy protein flour solution in embodiment 3 is 51.3% of that in the corresponding comparative example.
[0070] 3. Determination of the IgE-binding level of soy proteins
[0071] An indirect ELISA approach was used to test the IgE-binding ability of the soy proteins and reflect the changes of allergenicity in modified proteins:
[0072] A 96-well plate was coated with each saccharide modified hypoallergenic soy protein flour solution obtained in embodiments 1-3 (100 uL/well in 50 mM carbonate buffer, pH 9.6) at 4 °C overnight. The plate was washed and blocked with 5% bovine serum albumin (BSA, 200 pL/well) in 10 mM PBS (pH 7.4) for 2 h at 37 °C. Then, pooled sera (diluted 1:30) from soybean-allergic patients were added to the plate (100 puL/well) and further incubated at 37 °C for 1 h. The plate was washed and treated with HRP mouse anti-human IgE serum (diluted 1: 5000; 200 pL/well) for another 2 h at 37 °C. After repeated washing, TMB was added (100 uL/well) and reacted for 30 min at 37 °C. The reaction was stopped by adding 2 M
H:SO: (50 pL/well) and the absorbance was recorded at 450 nm using a microplate reader. Results were expressed as a percentage relative to the IgE-binding level of the unhydrolyzed control (SPI).
[0073] IgE-binding ability (%) = ODsampie/ODcontrot * 100%. In this expression, ODsampic and ODconro respectively represent the OD value of the sample group (including the oligo/polysaccharides and polyphenols) and the control group (untreated proteins).
[0074] Statistical analysis was performed using the software IBM SPSS Statistics 22.0. A p-value of <0.05 was considered significantly different. The graph was prepared with GraphPad Prism 8.
[0075] The results can be seen in Figure 3. The allergenicity of the saccharide modified hypoallergenic soy protein flour in embodiment 1 was reduced by 61.3% in comparison to the unprocessed soy protein flour. The allergenicity of the saccharide modified hypoallergenic soy protein flour in embodiment 2 was reduced by 45.7% in comparison to the unprocessed soy protein flour. The allergenicity of the saccharide modified hypoallergenic soy protein flour in embodiment 3 was reduced by 56.7% in comparison to the unprocessed soy protein flour. In respective embodiments, adding polyphenols did not obviously change the hypoallergenic effect of saccharide modification on soy proteins. This indicates that glycation of reactive amino acid residues could induce damages in the allergen epitopes, and that the polyphenol-allergenic protein complexes specifically reduced the formation of the AGEs while did not impact the low-allergenicity of the product.
[0076] Thus it can be known that, the present invention induced damaging in the allergenic epitopes of soybean allergens through combining covalent complexation by polyphenols and dry-heat glycation by oligo/polysaccharides. Due to the anti-oxidant effect of polyphenols and their quinone intermediates, and the steric-hindrance effect of oligo/polysaccharides, the generation of AGEs in the product was greatly suppressed, thus avoiding endogenous side products which are harmful to the human body. The allergenicity of the saccharide modified hypoallergenic soy protein flour prepared by the method of the present invention is decreased by 45.7%-61.3%, and at the same time, the content of the fluorescent AGEs was reduced by 58.9%-70.3%, and the content of CML was reduced by 39.7%-50.5%.
The present method is convenient and easily operated with an additional improvement effect, and the prepared soy protein flour features good flavors and safety, which can be readily commercialized the food industry.
[0077] In the description of the present invention, reference terms including “one embodiment”, “some embodiments”, “example”, “specific example” or “some examples” refer to that specific characteristics, structures, materials or features which are described in conjunction with the embodiment or example are included in at least one embodiment or example of the present invention. In the present description, the schematic expression of the above terms should not be construed as always aiming at identical embodiments or examples. Besides, the described specific characteristics, structures, materials or features may be combined in an appropriate way in any one of or more embodiments. In addition, those skilled in the art can blend and combine different embodiments or examples described in the present invention.
[0078] Although the embodiments of the present invention have been illustrated and described above, it can be understood that the previously described embodiments are exemplary, and cannot be construed as limiting the present invention. Those ordinarily skilled in the art can change, modify, replace and transform the previously described embodiments within the scope of the present invention.
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