CN107226838A - Oligopeptides γ Glu γ Glu γ Glu Ile, dense taste imparting agent, flavoring and preparation method thereof - Google Patents
Oligopeptides γ Glu γ Glu γ Glu Ile, dense taste imparting agent, flavoring and preparation method thereof Download PDFInfo
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- CN107226838A CN107226838A CN201710511222.3A CN201710511222A CN107226838A CN 107226838 A CN107226838 A CN 107226838A CN 201710511222 A CN201710511222 A CN 201710511222A CN 107226838 A CN107226838 A CN 107226838A
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- SNCKGJWJABDZHI-ZKWXMUAHSA-N gamma-Glu-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O SNCKGJWJABDZHI-ZKWXMUAHSA-N 0.000 title claims abstract description 45
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 21
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 21
- 235000019640 taste Nutrition 0.000 title claims abstract description 21
- 238000002360 preparation method Methods 0.000 title claims abstract description 9
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 17
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 10
- 150000001413 amino acids Chemical group 0.000 claims abstract description 9
- 239000000243 solution Substances 0.000 claims description 31
- 239000007788 liquid Substances 0.000 claims description 19
- 238000006243 chemical reaction Methods 0.000 claims description 15
- 108090000790 Enzymes Proteins 0.000 claims description 8
- 102000004190 Enzymes Human genes 0.000 claims description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 7
- 229940024606 amino acid Drugs 0.000 claims description 6
- 108090000279 Peptidyltransferases Proteins 0.000 claims description 5
- -1 gamma-glutamyl amine Chemical class 0.000 claims description 5
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 5
- 102000009127 Glutaminase Human genes 0.000 claims description 4
- 108010073324 Glutaminase Proteins 0.000 claims description 4
- UPCDLBPYWXOCOK-UHFFFAOYSA-N N-L-gamma-glutamyl-S-methyl-L-cysteine Natural products CSCC(C(O)=O)NC(=O)CCC(N)C(O)=O UPCDLBPYWXOCOK-UHFFFAOYSA-N 0.000 claims description 4
- 239000007864 aqueous solution Substances 0.000 claims description 4
- 238000010828 elution Methods 0.000 claims description 4
- RQNSKRXMANOPQY-BQBZGAKWSA-N gamma-Glu-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O RQNSKRXMANOPQY-BQBZGAKWSA-N 0.000 claims description 4
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 4
- FUZOZPRKGAXGOB-UHFFFAOYSA-N gamma-Glu-Abu Chemical compound CCC(C(O)=O)NC(=O)CCC(N)C(O)=O FUZOZPRKGAXGOB-UHFFFAOYSA-N 0.000 claims description 3
- JHFNSBBHKSZXKB-VKHMYHEASA-N Asp-Gly Chemical compound OC(=O)C[C@H](N)C(=O)NCC(O)=O JHFNSBBHKSZXKB-VKHMYHEASA-N 0.000 claims description 2
- OOULJWDSSVOMHX-WDSKDSINSA-N Cys-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CS OOULJWDSSVOMHX-WDSKDSINSA-N 0.000 claims description 2
- XUJNEKJLAYXESH-UWTATZPHSA-N D-Cysteine Chemical compound SC[C@@H](N)C(O)=O XUJNEKJLAYXESH-UWTATZPHSA-N 0.000 claims description 2
- FCQBDQYWNGUTPD-BQBZGAKWSA-N Gamma glutamyl ornithine Chemical compound NCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CCC(O)=O FCQBDQYWNGUTPD-BQBZGAKWSA-N 0.000 claims description 2
- SQBNIUOYNOKDTI-WHFBIAKZSA-N Gamma-glutamyl-Serine Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CO)C(O)=O SQBNIUOYNOKDTI-WHFBIAKZSA-N 0.000 claims description 2
- PABVKUJVLNMOJP-WHFBIAKZSA-N Glu-Cys Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CS)C(O)=O PABVKUJVLNMOJP-WHFBIAKZSA-N 0.000 claims description 2
- MFBYPDKTAJXHNI-VKHMYHEASA-N Gly-Cys Chemical compound [NH3+]CC(=O)N[C@@H](CS)C([O-])=O MFBYPDKTAJXHNI-VKHMYHEASA-N 0.000 claims description 2
- MYFMARDICOWMQP-UHFFFAOYSA-N L-L-gamma-Glutamylleucine Natural products CC(C)CC(C(O)=O)NC(=O)CCC(N)C(O)=O MYFMARDICOWMQP-UHFFFAOYSA-N 0.000 claims description 2
- AQAKHZVPOOGUCK-UHFFFAOYSA-N L-L-gamma-Glutamylvaline Natural products CC(C)C(C(O)=O)NC(=O)CCC(N)C(O)=O AQAKHZVPOOGUCK-UHFFFAOYSA-N 0.000 claims description 2
- ZUKPVRWZDMRIEO-VKHMYHEASA-N L-cysteinylglycine Chemical compound SC[C@H]([NH3+])C(=O)NCC([O-])=O ZUKPVRWZDMRIEO-VKHMYHEASA-N 0.000 claims description 2
- RITKHVBHSGLULN-WHFBIAKZSA-N L-gamma-glutamyl-L-cysteine Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(O)=O RITKHVBHSGLULN-WHFBIAKZSA-N 0.000 claims description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 2
- ACIJGUBIMXQCMF-UHFFFAOYSA-N N-L-gamma-glutamyl-glycine Natural products OC(=O)C(N)CCC(=O)NCC(O)=O ACIJGUBIMXQCMF-UHFFFAOYSA-N 0.000 claims description 2
- 108010047857 aspartylglycine Proteins 0.000 claims description 2
- 108010016616 cysteinylglycine Proteins 0.000 claims description 2
- WQXXXVRAFAKQJM-WHFBIAKZSA-N gamma-Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)CC[C@H](N)C(O)=O WQXXXVRAFAKQJM-WHFBIAKZSA-N 0.000 claims description 2
- ACIJGUBIMXQCMF-BYPYZUCNSA-N gamma-Glu-Gly Chemical compound OC(=O)[C@@H](N)CCC(=O)NCC(O)=O ACIJGUBIMXQCMF-BYPYZUCNSA-N 0.000 claims description 2
- MYFMARDICOWMQP-YUMQZZPRSA-N gamma-Glu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O MYFMARDICOWMQP-YUMQZZPRSA-N 0.000 claims description 2
- AQAKHZVPOOGUCK-XPUUQOCRSA-N gamma-Glu-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O AQAKHZVPOOGUCK-XPUUQOCRSA-N 0.000 claims description 2
- BBAYFIRFVORJLJ-UHFFFAOYSA-N gamma-Glutamyl-alpha-ornitine Natural products NCCCC(C(O)=O)NC(=O)CCC(N)C(O)=O BBAYFIRFVORJLJ-UHFFFAOYSA-N 0.000 claims description 2
- 108010064169 gamma-glutamyl-leucine Proteins 0.000 claims description 2
- 108010068906 gamma-glutamylcysteine Proteins 0.000 claims description 2
- 108010067681 gamma-glutamylornithine Proteins 0.000 claims description 2
- GWNXFCYUJXASDX-UHFFFAOYSA-N gamma-glutamylthreonine Chemical compound CC(O)C(C(O)=O)NC(=O)CCC(N)C(O)=O GWNXFCYUJXASDX-UHFFFAOYSA-N 0.000 claims description 2
- 108010032395 gamma-glutamylvaline Proteins 0.000 claims description 2
- 229960000310 isoleucine Drugs 0.000 claims description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 2
- DVCSNHXRZUVYAM-BQBZGAKWSA-N leu-asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O DVCSNHXRZUVYAM-BQBZGAKWSA-N 0.000 claims description 2
- 239000012295 chemical reaction liquid Substances 0.000 claims 1
- 150000002825 nitriles Chemical class 0.000 claims 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical class OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 abstract description 6
- 235000013305 food Nutrition 0.000 abstract description 2
- 102000004196 processed proteins & peptides Human genes 0.000 abstract 2
- 238000011156 evaluation Methods 0.000 description 12
- 230000001953 sensory effect Effects 0.000 description 12
- 125000002642 gamma-glutamyl group Chemical group 0.000 description 11
- 239000000796 flavoring agent Substances 0.000 description 9
- 235000019634 flavors Nutrition 0.000 description 9
- 230000000694 effects Effects 0.000 description 7
- 239000000463 material Substances 0.000 description 6
- 239000012071 phase Substances 0.000 description 6
- 239000000523 sample Substances 0.000 description 5
- XBJFCYDKBDVADW-UHFFFAOYSA-N acetonitrile;formic acid Chemical compound CC#N.OC=O XBJFCYDKBDVADW-UHFFFAOYSA-N 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 235000015278 beef Nutrition 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 235000014347 soups Nutrition 0.000 description 4
- 102100035650 Extracellular calcium-sensing receptor Human genes 0.000 description 3
- 101710159793 Extracellular calcium-sensing receptor Proteins 0.000 description 3
- 238000010811 Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry Methods 0.000 description 3
- 235000019606 astringent taste Nutrition 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 235000014705 isoleucine Nutrition 0.000 description 3
- 235000013555 soy sauce Nutrition 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 2
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N ammonia Natural products N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000000132 electrospray ionisation Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000002708 enhancing effect Effects 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 238000000703 high-speed centrifugation Methods 0.000 description 2
- 239000002054 inoculum Substances 0.000 description 2
- 150000002520 isoleucines Chemical class 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- LPUQAYUQRXPFSQ-DFWYDOINSA-M monosodium L-glutamate Chemical class [Na+].[O-]C(=O)[C@@H](N)CCC(O)=O LPUQAYUQRXPFSQ-DFWYDOINSA-M 0.000 description 2
- 235000013923 monosodium glutamate Nutrition 0.000 description 2
- 239000006199 nebulizer Substances 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 238000004321 preservation Methods 0.000 description 2
- 238000004451 qualitative analysis Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 235000015099 wheat brans Nutrition 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 101710159104 Flavor peptide Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- VVLXCWVSSLFQDS-UHFFFAOYSA-N N-L-gamma-glutamyl-L-tyrosine Natural products OC(=O)C(N)CCC(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 VVLXCWVSSLFQDS-UHFFFAOYSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 235000019632 basic taste sensations Nutrition 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 239000012496 blank sample Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000010668 complexation reaction Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000021107 fermented food Nutrition 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- HQVFCQRVQFYGRJ-UHFFFAOYSA-N formic acid;hydrate Chemical compound O.OC=O HQVFCQRVQFYGRJ-UHFFFAOYSA-N 0.000 description 1
- OWQDWQKWSLFFFR-WDSKDSINSA-N gamma-Glu-Glu Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(O)=O)CCC(O)=O OWQDWQKWSLFFFR-WDSKDSINSA-N 0.000 description 1
- VVLXCWVSSLFQDS-QWRGUYRKSA-N gamma-Glu-Tyr Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 VVLXCWVSSLFQDS-QWRGUYRKSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 235000019668 heartiness Nutrition 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000004223 monosodium glutamate Substances 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 210000000697 sensory organ Anatomy 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000004885 tandem mass spectrometry Methods 0.000 description 1
- 235000012976 tarts Nutrition 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000004704 ultra performance liquid chromatography Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1021—Tetrapeptides with the first amino acid being acidic
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
- A23L27/22—Synthetic spices, flavouring agents or condiments containing amino acids containing glutamic acids
-
- 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
- A23V2200/00—Function of food ingredients
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Nutrition Science (AREA)
- Seasonings (AREA)
Abstract
The invention discloses oligopeptides γ Glu γ Glu γ Glu Ile, dense taste imparting agent, flavoring and preparation method thereof.The amino acid sequence of the oligopeptides γ Glu γ Glu γ Glu Ile is γ Glu γ Glu γ Glu Ile.Dense taste imparting agent is made up of the oligopeptides and other peptides.The flavoring contains more than 300mg/kg γ Glu γ Glu γ Glu Ile.This γ glutamine peptides γ Glu γ Glu γ Glu Ile are remarkably improved the savoury of food particularly flavouring under 300mg/kg concentration.
Description
Technical field
The present invention relates to the peptide with flavor effect, and in particular to γ-Glutamyl Peptide and its application with savoury.
Background technology
γ-Glutamyl Peptide is deposited with a variety of animals and plants and fermented food, being that a kind of safety is natural extensively, safety food into
Point.Its primary structure of common glutathione is γ-Glu-Cys-Gly, is a kind of typical γ-Glutamyl Peptide.Modern study
Show that γ-Glutamyl Peptide is relevant with the metabolic activity and physiological function of organism, most of γ-Glutamyl Peptide has calm in addition
Depressurize, fatigue of releiving, anticancer removing toxic substances, complexation heavy metal ion, maintain cellular metal ions balance etc. physiological function.
In recent years, it has been found that γ-Glutamyl Peptide also has stronger flavor characteristic.Japanese aginomoto strain formula meeting in 2002
Society is disclosed by exploring the diversified compound with CaSR agonist activities, finds to assign with more excellent dense taste
Effect, the dense taste imparting effect particularly with preceding taste type, and with excellent stability, can be easy and produce at low cost
The material for being capable of imparting body taste with other there is CaSR to swash there is provided the dense taste imparting agent comprising the material, and by the material
The combinations of substances of dynamic agent activity using compound dense taste imparting agent.Include γ-Glu-Abu (L- gamma-glutamyl-L-2- ammonia
Base butyric acid) dense taste imparting agent, and the material with other have the combinations of substances of CaSR agonist activities using answer
Close dense taste imparting agent (number of patent application 201080024054.1).
Most of γ-Glutamyl Peptide under low consistency conditions has slight astringent taste, with the raising of concentration, γ-paddy ammonia
Acyl peptide starts that primary taste is presented.Such as γ-Glu-Glu have delicate flavour, γ-Glu-tyr bitter taste when concentration is 10mmol/L
Threshold value is twice of its astringent taste threshold value.In delicate flavour solution, γ-Glutamyl Peptide has savoury, and threshold value is also being decreased obviously.With
People further appreciate that scholar has found that γ-Glutamyl Peptide has the feature of savoury material to flavor peptide：1. base in aqueous
This insipidness or only slight taste (astringent taste or tart flavour)；2. increasing can be cooperateed with other taste compounds in system
Effect is acted on, and is added in the solution system containing delicate flavour material, will not change the basic taste sensation intensity of solution, but can coordinate each
Taste is planted, dense sense (kokumi) is dramatically increased；3. compared with pure water solution, threshold value is decreased obviously in delicate flavour solution.
Table 1 has reported γ-Glutamyl Peptide flavor characteristic and threshold value list
So far, there is not yet γ-Glu- γ-Glu- γ-Glu-Ile have the report of dense taste.
The content of the invention
It is an object of the invention to overcome deficiencies of the prior art, there is provided one kind utilization glutamine enzymatic synthesis
The preparation method of γ-Glutamyl Peptide.
The purpose of the present invention is achieved through the following technical solutions.
A kind of oligopeptides, its amino acid sequence is γ-Glu- γ-Glu- γ-Glu-Ile.
The dense taste imparting agent that the present invention is provided, is combined by the oligopeptides and more than one following peptide：γ-Glu-
X-Gly (X represents amino acid or amino acid derivativges), γ-Glu-Val-Y (Y represents amino acid or amino acid derivativges), γ-
Glu-Abu、γ-Glu-Ala、γ-Glu-Gly、γ-Glu-Cys、γ-Glu-Met、γ-Glu-Thr、γ-Glu-Val、γ-
Glu-Orn、Asp-Gly、Cys-Gly、Cys-Met、Glu-Cys、Gly-Cys、Leu-Asp、D-Cys、γ-Glu-Met(O)、
γ-Glu-γ-Glu-Val、γ-Glu-Val-NH2、γ-Glu-Val-ol、γ-Glu-Ser、γ-Glu-Tau、γ-Glu-
Cys (S-Me) (O), γ-Glu-Leu, γ-Glu-Ile, γ-Glu-t-Leu and γ-Glu-Cys (S-Me).
A kind of flavoring containing the oligopeptides, it contains more than 300mg/kg γ-Glu- γ-Glu- γ-Glu-
Ile。
A kind of flavoring containing the oligopeptides, the γ-Glu- γ-Glu- γ-Glu-Ile containing more than 1000mg/kg.
The preparation method of the oligopeptides, be specifically：Glutamine and free isoleucine, mol ratio is 1-2:1, it is dissolved in water
In solution, regulation reaction pH is 7.0-10.0, addition glutaminase or gamma-glutamyl amine transpeptidase 0.02-1% (w/w),
Reacted 3-12 hour at 25-50 DEG C, between the rear pH to 7~8 with 4mol/L hydrochloric acid readjustment, 90 DEG C of enzyme 10min that go out, obtain containing γ-
Glu- γ-Glu- γ-Glu-Ile reaction solution.Using 5 μm of 4.6x 250mm analytical columns of XSelect HSS T3, mobile phase A
Liquid is 0.1% (V/V) formic acid-aqueous solution；Mobile phase B liquid is 0.1% (V/V) formic acid-acetonitrile solution, and column temperature is 40 DEG C, flow velocity
For 1mL/min, the μ L of sample size 10 of reaction solution, gradient elution is carried out to reaction solution using high performance liquid chromatography, 9.671min goes out
Peak be oligopeptides γ-Glu- γ-Glu- γ-Glu-Ile.
Further, the concentration of the solution GLN is 400-1000mmol/L.
The present invention compared with prior art, has the following advantages that：
1) there is savoury characteristic present invention firstly discloses γ-Glu- γ-Glu- γ-Glu-Ile.
2) make public for the first time and utilize glutaminase or gamma-glutamyl amine transpeptidase catalytic preparation of gamma-Glu- γ-Glu-
γ-Glu-Ile。
Brief description of the drawings
Fig. 1 is the liquid chromatogram of mixture after enzymatic reaction；
Fig. 2 is γ-Glu- γ-Glu- γ-Glu-Ile second order mses figure.
Embodiment
Work further citing, but implementation of the invention and guarantor are specifically implemented to the present invention below in conjunction with accompanying drawing and example
Protect not limited to this.
Embodiment 1
By bacillus amyloliquefaciens (Bacillus amyloliquefaciens) SWJS22 (Chinese microorganism strain preservations
Administration committee's common micro-organisms center, deposit number is CGMCC No.8425, through in Chinese Patent Application No.
Have submitted preservation in 201510222162.4 application proves) fermentation medium (fermentation medium is inoculated in 1% inoculum concentration
Composition be：4% dregs of beans, 2% wheat bran, 2% corn flour) in, 37~39 DEG C of fermented and cultured 30h.By zymotic fluid in 4 DEG C,
High speed centrifugation 10min under the conditions of 10000r/min, filters to obtain supernatant, i.e. glutaminase crude enzyme liquid.
By 400mM glutamine and 600mM isoleucines in 100g water, the pH value of solution is adjusted respectively to 9.5, is added
1g crude enzyme liquids, after 40 DEG C respectively reaction 12h, are adjusted back after pH to 7.0,90 DEG C of enzyme 10min that go out are contained with 4mol/L hydrochloric acid
γ-Glu- γ-Glu- γ-Glu-Ile reaction solution.
Using 5 μm of 4.6x 250mm analytical columns of XSelect HSS T3, mobile phase A liquid is 0.1% (V/V) formic acid-water
Solution；Mobile phase B liquid is 0.1% (V/V) formic acid-acetonitrile solution, and column temperature is 40 DEG C, and flow velocity is 1mL/min, the sample introduction of reaction solution
10 μ L are measured, gradient elution (condition is carried out to reaction solution using high performance liquid chromatography：90% A liquid and 10% B liquid ladder during 0min
It is reduced in degree 5min in 85% A liquid and 15% B liquid, next 5min and is reduced to 20%A liquid and 80% B liquid).
9.671min peak is oligopeptides γ-Glu- γ-Glu- γ-Glu-Ile.9.671min oligopeptides peak is collected, sense organ is carried out and comments
Valency and UPLC-MS/MS analyses.
UPLC-MS/MS carries out qualitative analysis to reaction product：Including：An Agilent 1290series UPLC
System (Agilent Technologies) is used to separate each γ-Glu-peptides, with an elec-trospray
Ionization (ESI) mass spectrometer system (Q-TOF MS/MS, Bruker Daltonics) carries out qualitative analysis.Chromatographic column is：
Agilent ZORBAX RRHD SB-C18(2.1x 50mm,1.8μm).Sample size is 5 μ L.Liquid-phase condition is：Solution A is
0.1% formic acid-the aqueous solution, and solution B are 0.1% formic acid-acetonitrile solution, and gradient elution program is：0-10%B, 0-5.0min；
10-15%B, 5.0-10.0min；Then 100%B, 10.0-12.0min.MS conditions：Ionization (ionization)：Cation
Pattern；Drying gas (dry gas)：10L/min at 350 DEG C；Nebulizer (nebulizer pressure)：25psig；
Fragmentor (capillary voltage)：30V.UPLC-MS/MS analyses, its testing result such as Fig. 2 are carried out to gleanings.Can by Fig. 2
Know, its primary structure is γ-Glu- γ-Glu- γ-Glu-Ile.
Embodiment 2
Bacillus subtillis ATCC 6633 is inoculated in the fermentation medium (composition of fermentation medium with 1% inoculum concentration
For：4% dregs of beans, 2% wheat bran, 2% corn flour) in, 37~39 DEG C of fermented and cultured 48h.By zymotic fluid in 4 DEG C, 10000r/min
Under the conditions of high speed centrifugation 10min, filter to obtain supernatant, i.e. gamma-glutamyl amine transpeptidase crude enzyme liquid.
600mM glutamine and 400mM isoleucines are dissolved in 100g water, the pH value of solution is adjusted respectively to 8.0, plus
Enter 1g gamma-glutamyl amine transpeptidase crude enzyme liquids, after 40 DEG C respectively reaction 6h, adjusted back with 4mol/L hydrochloric acid after pH to 7.0,90 DEG C
Go out enzyme 10min, obtains the reaction solution rich in γ-Glu- γ-Glu- γ-Glu-Ile.Using 5 μm of XSelect HSS T3
4.6x 250mm analytical columns, mobile phase A liquid is 0.1% (V/V) formic acid-aqueous solution；Mobile phase B liquid be 0.1% (V/V) formic acid-
Acetonitrile solution, column temperature is 40 DEG C, and flow velocity is 1mL/min, the μ L of sample size 10 of reaction solution, using high performance liquid chromatography to reaction solution
Gradient elution is carried out, 9.671min oligopeptides peak is oligopeptides γ-Glu- γ-Glu- γ-Glu-Ile.
Embodiment 3
Add in 0.04% (g/g) γ-Glu- γ-Glu- γ-Glu- γ-Glu-Ile soy sauce, evaluate the change of its flavor characteristic
Change.Wherein, soy sauce is commercially available extra large day Gold Label soy.Sensory evaluation experiment had by 30-41 Sui 7 males of sensory evaluation experience with
9 women compositions.Analyses Methods for Sensory Evaluation Results shows, adds 0.04g% γ-Glu- γ-Glu- γ-Glu-Ile soy sauce, its savoury
It is respectively provided with and significantly improves.
Embodiment 4
0.04g and 0.08g γ-Glu- γ-Glu- γ-Glu-Ile, and 0.5g salt and 0.3g monosodium glutamates are weighed, is dissolved
Sensory evaluation is carried out in 100g water, and with blank sample (0.5g salt is dissolved in 100g water).Sensory evaluation is tested by 30-41 Sui
It is made up of 7 males and 9 women of sensory evaluation experience, Analyses Methods for Sensory Evaluation Results is shown in Table 1.
From table 1, threshold values of the γ-Glu- γ-Glu- γ-Glu-Ile in saline solution is 0.08g/100g, adds taste
The stimulation that essence can obviously reduce both γ-Glu- γ-Glu- γ-Glu-Ile is in taste threshold value, is 0.04g/100g.
Table 1
Have in 16 sensory evaluation groups 13 people find addition γ-Glu- γ in 0.5% salt and 0.3% monosodium glutamate solution-
Glu- γ-Glu-Ile sample has significant savoury enhancing effect, and 3 people think that savoury slightly has enhancing.
Embodiment 5
Beef is mixed with 9 times of weight deionized waters, 100 DEG C are boiled after 60min, filtering removes insoluble substance and oil
After fat, the salt for adding steamed beef soup weight 0.3%, add respectively the γ-Glu- γ of steamed beef soup weight 0.04% and 0.05%-
Glu- γ-Glu-Ile, and transfer to sensory evaluation group to evaluate the savoury of chicken soup, it the results are shown in Table 2.Sensory evaluation is tested
It is made up of by 30-41 Sui 11 males and 9 women of sensory evaluation experience,
Table 2
0.04-0.05% γ-Glu- γ-Glu- γ-Glu-Ile are added in table 2, steamed beef soup, more than 90%
Sensory evaluation group above thinks that savoury has significantly or is increased slightly.
Claims (7)
1. a kind of oligopeptides γ-Glu- γ-Glu- γ-Glu-Ile, it is characterised in that its amino acid sequence is γ-Glu- γ-Glu-
γ-Glu-Ile。
2. dense taste imparting agent, it is characterised in that combined as oligopeptides described in claim 1 and more than one following peptide：
γ-Glu-X-Gly、γ-Glu-Val-Y、γ-Glu-Abu、γ-Glu-Ala、γ-Glu-Gly、γ-Glu-Cys、γ-Glu-
Met、γ-Glu-Thr、γ-Glu-Val、γ-Glu-Orn、Asp-Gly、Cys-Gly、Cys-Met、Glu-Cys、Gly-Cys、
Leu-Asp、D-Cys、γ-Glu-Met(O)、γ-Glu-γ-Glu-Val、γ-Glu-Val-NH2、γ-Glu-Val-ol、
γ-Glu-Ser、γ-Glu-Tau、γ-Glu-Cys(S-Me)(O)、γ-Glu-Leu、γ-Glu-Ile、γ-Glu-t-Leu
With γ-Glu-Cys (S-Me)；X, Y represent amino acid or amino acid derivativges.
3. a kind of flavoring containing oligopeptides described in claim 1, it is characterised in that the γ-Glu- containing more than 400mg/kg
γ-Glu-γ-Glu-Ile。
4. flavoring according to claim 3, it is characterised in that the γ-Glu- γ-Glu- containing more than 1000mg/kg
γ-Glu-Ile。
5. the preparation method of oligopeptides described in claim 1, it is characterised in that glutamine and free isoleucine, mol ratio is 1-
2:1, soluble in water to obtain solution, regulation reaction pH is 7.0-10.0, addition glutaminase or gamma-glutamyl amine transpeptidase
0.02-1%（w/w）, reacted 3-12 hours at 25-50 DEG C, between the rear pH to 7 ~ 8 with 4 mol/L hydrochloric acid readjustment, 90 DEG C of enzymes 10 that go out
Min, obtains the reaction solution rich in γ-Glu- γ-Glu- γ-Glu-Ile.
6. the preparation method of oligopeptides according to claim 5, it is characterised in that：Using 5 μm of 4.6x of XSelect HSS T3
250mm analytical columns, mobile phase A liquid is 0.1%（V/V）Formic acid-the aqueous solution；Mobile phase B liquid is 0.1% (V/V) formic acid-second
Nitrile solution, column temperature is 40 DEG C, and flow velocity is 1 mL/min, the μ L of sample size 10 of reaction solution, using high performance liquid chromatography to reaction
Liquid carries out gradient elution, and the peak that 9.671min goes out is oligopeptides γ-Glu- γ-Glu- γ-Glu-Ile.
7. preparation method according to claim 5, it is characterised in that the concentration of the solution GLN is 400-
1000mmol/L。
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