CN105476012A - Formula food with special medical application and preparation method thereof - Google Patents
Formula food with special medical application and preparation method thereof Download PDFInfo
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- CN105476012A CN105476012A CN201510998050.8A CN201510998050A CN105476012A CN 105476012 A CN105476012 A CN 105476012A CN 201510998050 A CN201510998050 A CN 201510998050A CN 105476012 A CN105476012 A CN 105476012A
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- Prior art keywords
- lactalbumin
- peptide
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- accordance
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- 235000013305 food Nutrition 0.000 title claims abstract description 17
- 238000002360 preparation method Methods 0.000 title claims abstract description 15
- 102000004407 Lactalbumin Human genes 0.000 claims abstract description 99
- 108090000942 Lactalbumin Proteins 0.000 claims abstract description 99
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 69
- OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 claims abstract description 26
- PVNIIMVLHYAWGP-UHFFFAOYSA-N Niacin Chemical compound OC(=O)C1=CC=CN=C1 PVNIIMVLHYAWGP-UHFFFAOYSA-N 0.000 claims abstract description 22
- 239000003814 drug Substances 0.000 claims abstract description 19
- 238000000034 method Methods 0.000 claims abstract description 18
- OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 claims abstract description 13
- 229960000304 folic acid Drugs 0.000 claims abstract description 13
- 235000019152 folic acid Nutrition 0.000 claims abstract description 13
- 239000011724 folic acid Substances 0.000 claims abstract description 13
- 239000000203 mixture Substances 0.000 claims abstract description 11
- 235000001968 nicotinic acid Nutrition 0.000 claims abstract description 11
- 229960003512 nicotinic acid Drugs 0.000 claims abstract description 11
- 239000011664 nicotinic acid Substances 0.000 claims abstract description 11
- 239000004365 Protease Substances 0.000 claims description 28
- 239000000725 suspension Substances 0.000 claims description 26
- 102000007544 Whey Proteins Human genes 0.000 claims description 20
- 108010046377 Whey Proteins Proteins 0.000 claims description 20
- 108091005804 Peptidases Proteins 0.000 claims description 18
- 102000035195 Peptidases Human genes 0.000 claims description 18
- 235000021119 whey protein Nutrition 0.000 claims description 15
- 239000002131 composite material Substances 0.000 claims description 13
- 235000019419 proteases Nutrition 0.000 claims description 13
- 102000009027 Albumins Human genes 0.000 claims description 12
- 108010088751 Albumins Proteins 0.000 claims description 12
- 235000013336 milk Nutrition 0.000 claims description 12
- 239000008267 milk Substances 0.000 claims description 12
- 210000004080 milk Anatomy 0.000 claims description 12
- 150000001875 compounds Chemical class 0.000 claims description 11
- 108090000526 Papain Proteins 0.000 claims description 10
- 235000019834 papain Nutrition 0.000 claims description 10
- 229940055729 papain Drugs 0.000 claims description 10
- 235000005911 diet Nutrition 0.000 claims description 8
- 230000000378 dietary effect Effects 0.000 claims description 8
- 238000005507 spraying Methods 0.000 claims description 8
- 241001465754 Metazoa Species 0.000 claims description 5
- 102000057297 Pepsin A Human genes 0.000 claims description 5
- 108090000284 Pepsin A Proteins 0.000 claims description 5
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 claims description 5
- 239000002249 anxiolytic agent Substances 0.000 claims description 5
- 229940111202 pepsin Drugs 0.000 claims description 5
- 235000018102 proteins Nutrition 0.000 claims description 4
- 102000004169 proteins and genes Human genes 0.000 claims description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 4
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- 102000005158 Subtilisins Human genes 0.000 claims description 3
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- 230000000049 anti-anxiety effect Effects 0.000 claims description 3
- 235000019835 bromelain Nutrition 0.000 claims description 3
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- 239000000796 flavoring agent Substances 0.000 claims description 2
- 235000019634 flavors Nutrition 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 12
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- 229920001184 polypeptide Polymers 0.000 abstract description 9
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- 229940079593 drug Drugs 0.000 abstract description 4
- 235000016709 nutrition Nutrition 0.000 abstract description 3
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- 238000010521 absorption reaction Methods 0.000 abstract description 2
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- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 12
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- 239000005862 Whey Substances 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
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- AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 description 4
- 229960003529 diazepam Drugs 0.000 description 4
- JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 210000000481 breast Anatomy 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 101000984728 Chiropsoides quadrigatus Angiotensin-converting enzyme inhibitory peptide Proteins 0.000 description 2
- 102000002265 Human Growth Hormone Human genes 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 239000000854 Human Growth Hormone Substances 0.000 description 2
- 102000014171 Milk Proteins Human genes 0.000 description 2
- 108010011756 Milk Proteins Proteins 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000949 anxiolytic effect Effects 0.000 description 2
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- 238000011088 calibration curve Methods 0.000 description 2
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- 230000006870 function Effects 0.000 description 2
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- 229960000890 hydrocortisone Drugs 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 235000021239 milk protein Nutrition 0.000 description 2
- 230000000116 mitigating effect Effects 0.000 description 2
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 206010063659 Aversion Diseases 0.000 description 1
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 206010016275 Fear Diseases 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- 206010022998 Irritability Diseases 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 244000225942 Viola tricolor Species 0.000 description 1
- 235000004031 Viola x wittrockiana Nutrition 0.000 description 1
- YAJCHEVQCOHZDC-QMMNLEPNSA-N actrapid Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3N=CNC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@H](C)CC)[C@H](C)CC)[C@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C(N)=O)C1=CNC=N1 YAJCHEVQCOHZDC-QMMNLEPNSA-N 0.000 description 1
- 230000003712 anti-aging effect Effects 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003064 anti-oxidating effect Effects 0.000 description 1
- 230000002785 anti-thrombosis Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 230000002567 autonomic effect Effects 0.000 description 1
- 235000008452 baby food Nutrition 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 229910052796 boron Inorganic materials 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- LEMUFSYUPGXXCM-JNEQYSBXSA-N caninsulin Chemical compound [Zn].C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC3N=CN=C3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1C=NC=N1 LEMUFSYUPGXXCM-JNEQYSBXSA-N 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 230000002526 effect on cardiovascular system Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000021824 exploration behavior Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 235000013402 health food Nutrition 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 235000021125 infant nutrition Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229960005181 morphine Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000010606 normalization Methods 0.000 description 1
- 235000003170 nutritional factors Nutrition 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
-
- 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
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/435—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having six-membered rings with one nitrogen as the only ring hetero atom
- A61K31/44—Non condensed pyridines; Hydrogenated derivatives thereof
- A61K31/455—Nicotinic acids, e.g. niacin; Derivatives thereof, e.g. esters, amides
-
- 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
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/495—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having six-membered rings with two or more nitrogen atoms as the only ring heteroatoms, e.g. piperazine or tetrazines
- A61K31/505—Pyrimidines; Hydrogenated pyrimidines, e.g. trimethoprim
- A61K31/519—Pyrimidines; Hydrogenated pyrimidines, e.g. trimethoprim ortho- or peri-condensed with heterocyclic rings
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
The invention provides a formula food with special medical application and a preparation method thereof, and application of the formula food in preparation of a medical drug. The prepared lactalbumin small peptide contains folic acid accounting for one millionth to one ten thousandth of the lactalbumin peptide by mass and nicotinic acid accounting for one thousandth to five thousandths of the lactalbumin peptide by mass; the lactalbumin peptide with molecular weight smaller than 1000 Dalton accounts for more than or equal to 98%. The product has the characteristics of high activity, high absorption rate, high nutrition, high safety and no side effect. By adopting the method, the lactalbumin is subjected to sufficient enzymolysis, the lactalbumin peptide yield is high, the prepared lactalbumin pepetide is a polypeptide mixture consisting of 2-5 amino acids and is easy to absorb by the organism, the sensitization property is further reduced, and the product activity is high; and the preparation method is simple to operate and suitable for industrial production.
Description
Technical field
The invention belongs to biochemical field, relate to a kind of special medicine purposes formula food and preparation method thereof, and it prepares the purposes of Medicines, particularly relate to a kind of by lactalbumin is carried out enzymolysis, the whey protein peptide prepared, with and preparation method thereof with a kind of purposes preparing Medicines.
Background technology
The research of breast source biologically active peptide starts from 1979, and the people such as the Brantl of Germany obtain some polypeptide products by enzymolysis bovine casein, and it is active to prove that they have class morphine, and from then on people expand the research of biologically active peptide aspect.Through the exploration of nearly 20 years, up to the present, multiple newborn source biologically active peptide has been had been found that.Comparatively deep to the ace inhibitory peptide research of milk protein sources abroad, especially Japan has carried out more research to the ace inhibitory peptide derived from lactalbumin, casein and Yoghourt, achieves larger progress.Domestic at the early-stage to research in this respect at present.Lactalbumin is the protein in the liquid by-product whey in industrial production cheese or casein process.It has, and absorptivity is high, fat is extremely low with contents of saccharide, simultaneously containing features such as abundant sulfur-containing amino acid, has and improves the health care such as cardiovascular, diabetes, infant nutrition, anti-ageing, raising immunity.Lactalbumin forms with the protein of its high-quality, and high biological utilisation is worth and special physiological function, is subject to international extensive concern, having a extensive future in sport nutrition, health care and food processing etc.
At present lactalbumin research is mainly concentrated in the research of whey protein fraction analysis, the preparation of whey polysaccharide polypeptide, enzymolysis process and antioxidation activity.Containing the biologically active peptide of a large amount of different activities in lactalbumin, these peptides naturally be present in lactalbumin or come from lactoprotein be hydrolyzed after product, due to its molecular weight, can the form of complete peptide section be absorbed by the body in small intestine.Lactalbumin, through protease hydrolytic, can not only significantly improve its dissolubility, stability, emulsibility, frothing capacity etc., and the peptide section produced after degraded is easier to the absorption of body, transhipment and utilization.In addition, by some sensitization structures effectively can be destroyed to the enzymolysis of lactalbumin, thus eliminate its sensitization, the immunological rejection of human body can not be caused, and there is multiple special physiological active functions.
Lactalbumin obtains Small molecular whey protein peptide through protease hydrolyzed, the mixtures of polypeptides that whey protein peptide is mainly made up of 2-7 amino acid, it is a kind of multifunctional and nutritional factor, there is immunological regulation, antithrombotic, anti-hypertension, norcholesterol, the multiple physiological active functions such as antibacterial, can be made into natural hypotensor, patient's nutritional supplement, infant food, old people food, sports food and various functional health foods etc., can the industries such as food and medicine be widely used in.
At present, the preparation of breast source biologically active peptide mainly adopts enzymatic isolation method, the proteolytic enzyme used is based on single enzyme, mainly contain trypsase, pepsin, alkali protease, neutral proteinase, papain etc., and the preparation of biologically active peptide for most of milk protein sources, the standby biologically active peptide content of single enzyme legal system is low, and isolation andpurification difficulty is large.Also some are had to produce the research report of whey protein peptide about composite protease hydrolysis lactalbumin both at home and abroad, but also mainly with the two kinds or more of enzyme associatings of above-mentioned trypsase, pepsin, alkali protease, neutral proteinase, papain, expect the content improving hydrolysis result and improve polypeptide.But still there is complex operation in above-mentioned all methods, starting whey protein concentration is too low, active peptide productive rate is low, high in cost of production defect.The suitability for industrialized production of breast source biologically active peptide also has certain difficulty.
The content of invention
For solving the problem, the invention provides a kind of special medicine purposes dietetic food, wherein comprise quality be whey protein peptide 1,000,000/to ten thousand/ folic acid and quality be the nicotinic acid of whey protein peptide one thousandth to thousand/five, molecular weight is less than 1000 daltonian whey protein peptides and reaches more than 98%.
For solving the problem, present invention also offers a kind of method preparing above-mentioned special medicine purposes dietetic food, it is characterized in that comprising the following steps:
(1) preparation quality percentage is the lactalbumin suspension of 1%-25%;
(2) add in lactalbumin suspension quality be lactalbumin 1,000,000/to ten thousand/ folic acid or the nicotinic acid of one thousandth to thousand/five;
(3) in lactalbumin suspension, add compound protease and carry out enzymolysis;
(4) by concentrated after compound protein enzyme-deactivating;
(5) product after concentrated is carried out spraying dry, obtain Composite Milk albumin peptide product.
Wherein, the concentration preferred mass percentage of described lactalbumin suspension is 5%-20%.
Wherein, the concentration of described folic acid preferably 1/100000th five to ten 5/10000ths.
Wherein, the content of the compound protease described in step (3) is 0.1% one 1% of lactalbumin amount.
Wherein, the compound protease described in step (3) is made up of any two or more in subtilopeptidase A (BiopraseSP-20), endotrypsin DenazymeAP, papain, flavor protease, bromelain, trypsase, neutral proteinase, animal proteolytic enzyme, acid protease and pepsin.
Wherein, the composition of two kinds of described compound proteases is according to (1-5): the part by weight composition of (5-1), preferably according to (1-3): the part by weight composition of (3-1), preferably according to (1-2): the part by weight composition of (2-1).
Wherein, the time of the enzymolysis of step (3) is 1-10 hour.
For solving the problem, present invention also offers the purposes that a kind of special medicine purposes dietetic food is used for the treatment of phrenoblabia, there is medical application antianxity.
For solving the problem, the dietetic food that present invention also offers a kind of above-mentioned special medicine purposes or the product prepared according to said method, for the preparation of the purposes of the medicine for the treatment of phrenoblabia, are particularly useful for the medicine preparing antianxiety purposes.
Product involved in the present invention has high activity, high-absorbility, high nutrition, high security, the feature had no side effect.The method that the present invention relates to can make the abundant enzymolysis of lactalbumin, whey protein peptide productive rate is high, obtained whey protein peptide is mainly the mixtures of polypeptides be made up of 2 ~ 5 amino acid and forms, be highly susceptible to body to absorb, Product Activity is higher, and the abundant thorough enzymolysis of lactalbumin destroys some sensitization structures, thus reduce its sensitization further, reduce the possibility that lactalbumin causes human immunity rejection, and preparation method is simple to operate, is suitable for the application of suitability for industrialized production.
Detailed description of the invention
Below in conjunction with specific embodiment, the invention will be further elaborated.But these embodiments are only exemplary, do not form any restriction to scope of the present invention.It will be understood by those skilled in the art that and can modify to the details of technical solution of the present invention and form or replace down without departing from the spirit and scope of the present invention, but these amendments and replacement all fall within the scope of protection of the present invention.
(1) assay method introduction:
1. peptide molecular weight distribution determination method
Adopt molecular weight and the content of high performance gel filtration chromatography determination and analysis gained whey polypeptide.
Determining instrument and method:
(1) chromatographic condition: chromatographic column: TSKGEL2000SW × L (specification 7.8mm × 300mm × 5um); Mobile phase: trifluoroacetic acid: acetonitrile: water=0.07:15:85; Determined wavelength: 214nm; Applied sample amount: 20 μ L; Flow velocity: 0.5mUmin.
(2) making of calibration curve: molecular weight standards is made into the standard solution that mass concentration is 5mg/mL with mobile phase take relative retention time as abscissa, and the logarithm of molecular weight is ordinate, makes calibration curve.
(3) mensuration of whey polypeptide molecular weight distribution: get whey polypeptide sample 0.5mg to be measured, add the solution that mobile phase is diluted to 5mg/mL, miillpore filter (0.45um) makes need testing solution after filtering.Content is calculated with area normalization method; According to relative retention time, reference standard curve, calculates molecular weight.
2. hydrolyzed whey protein degree assay method
(1) assay method (microdiffusion) of soluble nitrogen in solution
Get lactalbumin enzymolysis clarified solution 5ml, add 1g and digest catalyst and the 10ml concentrated sulfuric acid, at high temperature digest to yellow green, take out and be cooled to room temperature, add water constant volume.Then get the mistress that 5ml joins diffusion boat, and room adds the BAS of 2ml in diffusion boat, in mistress, add 4ml concentrated NaOH solution, and cover cover plate rapidly.Place after about 24h in natural conditions, with the hydrochloric acid solution titration of boron acid solution of standard to pansy.
Content (%)=(V
2-V
l) × NH × 0.014 × extension rate/example weight × 100%
Note:
V
l: blank required hydrochloric acid solution volume (ml);
V
2: titration liquid usage standard acid volume (ml) to be measured;
NH: standard acid normality;
The grams of 0.014Iml equivalent nitrogen.
(2) assay method-trichloroacetic acid method of degree of hydrolysis
Get in 10ml zymolyte and add 10ml trichloroacetic acid, heat 20min in a water bath, then centrifugal 15min under 4000r/min rotating speed.
Degree of hydrolysis is common to be defined as: degree of hydrolysis (DH)=(the total peptide bond number in the peptide bond number/raw material be hydrolyzed) × 100%, also can be expressed as degree of hydrolysis (DH)=(nitrogen content of the nitrogen content-blank sample of lactalbumin after enzymolysis)/(lactalbumin is without the nitrogen content of the nitrogen content-blank sample of enzymolysis)
(2) test material
Lactalbumin buying is from Henan Ji Mei Chemical Co., Ltd. and NZMP of New Zealand; Pepsin 1,200,000 u/g, trypsase 2,500,000 u/g (Chemical Reagent Co., Ltd., Sinopharm Group); Bromelain 850,000 u/g, papain 800,000 u/g (Pang Bo bio tech ltd, Nanning), neutral proteinase 2,000,000 u/g (the biochemical Co., Ltd in Baofeng, Shanghai); Subtilopeptidase A (BiopraseSP-20), endotrypsin DenazymeAP can from NegaseChemte × purchases; Standard molecular weight reagent ribalgilase, actrapid monotard, human growth hormone (HGH) release inhibiting factor are Chinese pharmaceutical biological product calibrating product.
(3) embodiment
Embodiment 1
Take 50g lactalbumin, aquation, be mixed with the lactalbumin suspension of 1.0wt%, in lactalbumin suspension, add quality is the millionth folic acid of lactalbumin amount and the nicotinic acid of 5/1000ths, adds the trypsase that quality is 0.1% of lactalbumin amount and papain (forming according to the part by weight of 2:1) in lactalbumin suspension.Under 45 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 1h.After testing, the degree of hydrolysis of lactalbumin is 36.5%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 20min, makes enzyme deactivation.Controlled hydrolysis degree, then the lactalbumin peptide solution of gained is concentrated, spraying dry, controls EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 40ml/min, obtains Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 98.5%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 99%.
Embodiment 2
Take 50g lactalbumin, aquation, be mixed with 5.0wt% lactalbumin suspension, the folic acid of 5/100000ths and the nicotinic acid of 3/1000ths that quality is lactalbumin amount is added in lactalbumin suspension, BiopraseSP-20 and the papain (formed according to the part by weight of 3:1) of lactalbumin amount 0.2% is added in lactalbumin suspension, under 40 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 6h.After testing, the degree of hydrolysis of lactalbumin is 41.2%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 20min, make enzyme deactivation, controlled hydrolysis degree, then the lactalbumin peptide solution of gained is concentrated, spraying dry, control EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 20ml/min obtain Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 96.1%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 98%.
Embodiment 3
Take 50g lactalbumin, aquation, be mixed with 20.0wt% lactalbumin suspension, the folic acid that quality is 5/100000ths of lactalbumin amount and millesimal nicotinic acid is added in lactalbumin suspension, BiopraseSP-20 and the papain (formed according to the part by weight of 1:1) of lactalbumin amount 0.5% is added in lactalbumin suspension, under 50 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 8h.After testing, the degree of hydrolysis of lactalbumin is 47.3%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 20min, make enzyme deactivation, controlled hydrolysis degree, then the lactalbumin peptide solution of gained is concentrated, spraying dry, control EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 10ml/min obtain Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 99.0%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 99%.
Embodiment 4
Take 50g lactalbumin, aquation, be mixed with 25.0wt% lactalbumin suspension, add in lactalbumin suspension quality be lactalbumin amount ten thousand/ folic acid and 2/1000ths nicotinic acid, BiopraseSP-20 and DenazymeAP (formed according to the part by weight of 5:1) of lactalbumin amount 1% is added in lactalbumin suspension, under 55 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 10h.After testing, the degree of hydrolysis of lactalbumin is 52.4%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 20min, make enzyme deactivation, controlled hydrolysis degree, then concentrated, spraying dry, control EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 10ml/min obtain Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 96.5%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 99%.
Embodiment 5
Take 50g lactalbumin, aquation, be mixed with 15.0wt% lactalbumin suspension, in lactalbumin suspension, add quality is the folic acid of 6/100000ths of lactalbumin amount and the nicotinic acid of 5/1000ths, BiopraseSP-20 and the papain (formed according to the part by weight of 3:2) of lactalbumin amount 2% is added in lactalbumin suspension, under 60 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 7h.After testing, the degree of hydrolysis of lactalbumin is 59.1%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 10min, make enzyme deactivation, controlled hydrolysis degree, then concentrated by the lactalbumin peptide solution of gained, spraying dry, control EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 40ml/min obtain Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 98.5%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 99%.
Embodiment 6
Take 50g lactalbumin, aquation, be mixed with 10.0wt% lactalbumin suspension, in lactalbumin suspension, add quality is the folic acid of 2/100000ths of lactalbumin amount and the nicotinic acid of 5/1000ths, BiopraseSP-20 and the papain (formed according to the part by weight of 1:2) of lactalbumin amount 0.4% is added in lactalbumin suspension, under 65 DEG C of constant temperatures, in constant temperature enzymatic vessel, obtain complete clear solution after enzyme hydrolysis 9h.After testing, the degree of hydrolysis of lactalbumin is 49.6%, then reaction system lactalbumin enzyme hydrolyzate rapid temperature increases to 100 DEG C is kept 20min, make enzyme deactivation, controlled hydrolysis degree, then concentrated, spraying dry, control EAT 190 DEG C, leaving air temp 95 DEG C, feed rate 20ml/min obtain Powdered Composite Milk albumin peptide product.After testing, the lactalbumin peptide content (in butt) prepared by the present embodiment reaches 99.5%; Peptide molecular weight distribution is: be less than 1000 and daltonianly account for 99%.
Embodiment 7
The present embodiment is by carrying out elevated plus-maze model (ElevatedPlusMaze is called for short EPM) test to animal, the present invention is to the regulating action of psychiatric system in research.Elevated plus-maze has in Small rodent animal anxiety test to be applied the most widely, and this system is used for detecting after taking anxiolytic, can reduce animal innately to height and the situation of vacant lot aversion.Rodent (such as rat, mouse) has exploratory behavior, and putting into after Elevated plus-maze can initiative exploring open arms, but fears in open arms and uphang unlimited environment.Anxiolytic drugs can increase open arms inquiry activity, causes anxiety agent then contrary.
Elevated plus-maze has a pair open arms and a pair closure arm.Test mice is divided into 6 groups, often organizes 10 mouse, give respectively and often organize the lactalbumin peptide product that test mice takes lactalbumin, diazepam (DZP), embodiment 1-6, taking dose sees the following form 1.The central platform place of EPM is placed in rapidly after test mice being adapted to a period of time, make its head just to wherein 1 open arms, the following data of following the tracks of in shooting record 5min are adopted also to calculate the mean value often organizing test data: 1. to enter open arms number of times (openarmentry, OE): the number of times entering into arbitrary open arms, all enter in arm with rat four claws and be as the criterion, the claw in midway exits completely from this arm, completes for this time activity of entering; 2. the open arms time (openarmtime, OT) is entered: the time entering open arms, unit was remembered with second; 3. enter closure arm number of times (closearmentry, CE): the number of times entering arbitrary closure arm, all enter in arm with rat four claws and be as the criterion; 4. the closure arm time (closearmentry, CT) is entered: the time entering closure arm, unit was remembered with second.By 1.-4. calculate respectively, result of the test sees the following form 1:
1. the total degree (OE+CE) of open arms and closure arm is entered: the motion activity representing rat;
2. open arms number of times ratio (OE%) is entered: namely open arms enters number of times/(OE+CE) × 100%;
3. open arms time of staying ratio (OT%), namely open arms the time of staying/(OT+CT) × 100%.
OE% and OT% represents angst resistance effect index, and it is more obvious to be worth the mitigation of larger expression antianxiety.
Table 1: the result of Composite Milk albumin peptide product in mouse EPM tests
Data are expressed as mean+SD (n=10). and (*: represent and compare p < 0.05 with negative control group)
Result of the test shows: when taking Composite Milk albumin peptide product and diazepam (DZP) to test mice, always enter arm number of times OE+CE, OT% and OE% value to increase than when taking lactalbumin, and the dosage taking compound whey protein peptide is larger, corresponding value is higher.Test shows: Composite Milk albumin peptide product has significant angst resistance effect (P < 0.05) on this Anxiety Model.Composite Milk albumin peptide product has certain mitigation to the animal anxiety caused by irritability model, significantly can reduce level of serum cortisol (level of serum cortisol is the important biochemical indicator of pressure state) under emergency rating, the present invention under foreign environment during mouse autonomic activities central nervous system over-activity have certain inhibitory action.
Claims (10)
1. a dietetic food for special medicine purposes, wherein comprise quality be whey protein peptide 1,000,000/to ten thousand/ folic acid and quality be the nicotinic acid of whey protein peptide one thousandth to thousand/five.
2. a kind of special medicine purposes dietetic food according to claim 1, is characterized in that its middle-molecular-weihydroxyethyl is less than 1000 daltonian lactalbumin peptide contents and reaches more than 98%.
3. prepare a dietetic food method for special medicine purposes according to claim 1, it is characterized in that comprising the following steps:
(1) preparation quality percentage is the lactalbumin suspension of 1%-25%;
(2) add in lactalbumin suspension quality be lactalbumin 1,000,000/to ten thousand/ folic acid and the nicotinic acid of one thousandth to thousand/five;
(3) in lactalbumin suspension, add compound protease and carry out enzymolysis;
(4) by concentrated after compound protein enzyme-deactivating;
(5) product after concentrated is carried out spraying dry, obtain Composite Milk albumin peptide product.
4. the concentration preferred mass percentage that in accordance with the method for claim 3, it is characterized in that the lactalbumin suspension described in step (1) is 5%-20%.
5. the concentration that in accordance with the method for claim 3, it is characterized in that step (2) described folic acid preferably 1/100000th five to ten 5/10000ths.
6. in accordance with the method for claim 3, it is characterized in that the content of the compound protease described in step (3) is 0.1% one 1% of lactalbumin amount.
7. in accordance with the method for claim 3, it is characterized in that the compound protease described in step (3) is made up of any two or more in subtilopeptidase A (BiopraseSP-20), endotrypsin DenazymeAP, papain, flavor protease, bromelain, trypsase, neutral proteinase, animal proteolytic enzyme, acid protease and pepsin.
8. in accordance with the method for claim 7, it is characterized in that the composition of two kinds of described compound proteases is according to (1-5): the part by weight composition of (5-1), preferably according to (1-3): the part by weight composition of (3-1), especially preferred according to (1-2): the part by weight composition of (2-1).
9. in accordance with the method for claim 3, it is characterized in that the time of the enzymolysis of step (3) is 1-10 hour.
10. product prepared by the dietetic food of the special medicine purposes according to any one of claim 1-2 or the method according to any one of claim 3-9, for the preparation of the purposes of the medicine for the treatment of phrenoblabia, is particularly useful for the medicine preparing antianxiety purposes.
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Effective date of registration: 20200108 Address after: 236600 Building 5, harmony Road, Taihe Economic Development Zone, Fuyang, Anhui Patentee after: CHINJANE MEDICAL FOOD CO., LTD. Address before: 236600 Building 5, harmony Road, Taihe Economic Development Zone, Fuyang, Anhui Co-patentee before: Guangzhou Health Medicine Development Co., Ltd. Patentee before: CHINJANE MEDICAL FOOD CO., LTD. |