CN106282284A - Stichopus japonicus oligopeptide production enzyme and enzymolysis process - Google Patents
Stichopus japonicus oligopeptide production enzyme and enzymolysis process Download PDFInfo
- Publication number
- CN106282284A CN106282284A CN201610654567.XA CN201610654567A CN106282284A CN 106282284 A CN106282284 A CN 106282284A CN 201610654567 A CN201610654567 A CN 201610654567A CN 106282284 A CN106282284 A CN 106282284A
- Authority
- CN
- China
- Prior art keywords
- stichopus japonicus
- enzyme
- enzymolysis
- enzymolysis process
- accounts
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
- C12N9/62—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi from Aspergillus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6472—Cysteine endopeptidases (3.4.22)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/94—Pancreatin
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/15—Peptidyl-dipeptidases (3.4.15)
- C12Y304/15001—Peptidyl-dipeptidase A (3.4.15.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21014—Microbial serine proteases (3.4.21.14)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/22—Cysteine endopeptidases (3.4.22)
- C12Y304/22002—Papain (3.4.22.2)
Abstract
The invention discloses Stichopus japonicus oligopeptide production enzyme and enzymolysis process, belong to Stichopus japonicus oligopeptide technical field of producing；On the basis of single enzyme screening, constituted the Stichopus japonicus enzymolysis specific complex protease including that restriction endonuclease and excision enzyme are made up of four kinds of enzymes by optimization；Zymoexciter is added in compound protease；Stichopus japonicus slurry carries out pretreatment after adjusting temperature and PH；Appropriate pretreating agent is added before pretreatment.It is reasonable in design, few by enzyme amount, enzymolysis time is short, enzymolysis yield high.Products taste is good, the most bitter or the slightest bitterness and fishy smell.
Description
Technical field
The present invention relates to Stichopus japonicus oligopeptide technical field of producing, be specifically related to Stichopus japonicus oligopeptide production enzyme and enzymolysis
Technique.
Background technology
Stichopus japonicus is China's traditional methods to keep in good health's recipe." food book on Chinese herbal medicine " author Yao that the Ming Dynasty publishes can achieve the expenditure main complement of Stichopus japonicus
Gas, grow the suitable vital organs of the human body and the health-preserving function [1994:695] dispelling deficient.In Qing Dynasty's " Bencao Congxin ", supplementary Amplifications of the Compendium of Materia Medica etc.
Stichopus japonicus is then classified as tonification medicine [1955:495] by pharmacopeia nationality.
Summarize according to Wu Yiluo, ZHAO Xue-Min etc.: Stichopus japonicus taste temperature is sweet salty, enters heart kidney channel.There are raw hundred arteries and veins blood, the kidney invigorating and essence nourishing, strong
The several functions such as sun treats fistula, disease of dispelling except labor, nourishing YIN to promote diuresis, correction softening the hard mass and logical intestinal are moisturized.
According to modern scientific research, Stichopus japonicus mainly contains the multiple biologies such as collagen protein, Stichopus japonicus polysaccharide and selenka
Active substance, and these bioactive substances all have more special structure, and this is also that Stichopus japonicus has multiple bioactive material
Basis [Fan Huizeng, 2001].
Collagen molecules amount in Stichopus japonicus must be dropped through the digestive organs of self at 1,000,000-120 ten thousand Da, human body
Solve as could absorbing by body after the oligopeptide of molecular weight ＜ 1000Da or aminoacid.Therefore digestibility is relatively low.Offset
The old people that the change the most unsound Children and teenager of allelotaxis, digestive function go down, gastrointestinal function weakens or postoperative patient
The utilization digesting and assimilating Stichopus japonicus is in order to improve above-mentioned crowd to Stichopus japonicus digestibility, and scientific research personnel manages in vitro with raw
Thing engineering way carries out pre-enzymolysis to Stichopus japonicus and becomes small-molecular peptides.As Su Yongchang etc. uses neutral protease As1398 to Fujian fresh sea cucumber
Being hydrolyzed, yield is 6.9%[2009]；Fresh the Liao Dynasty ginseng is hydrolyzed by the neutral protease As1398 such as Zhang Huo, and hydrolysis reaches
43.6%, molecular weight ＜ 2600Da content reaches 1.76%, accounts for total protein 22%[2001]；The thorn fresh to Yantai Zhifu Island such as Wang Hongtao
Ginseng As1398 neutral protease carries out enzymolysis, and polypeptide yield reaches 12%, hydrolyzes 30.35%[2006]；Huang Weibo etc. are to Guangdong
Zhanjiang fresh sea cucumber As1398 neutral protease and papain 1: 1 are hydrolyzed, and soluble protein yield reaches 69.2%
【2010】；Dong Huiming etc. have carried out enzymolysis, polypeptide yield 14.7% to Bohai Sea Gulf, Dalian Radix Morinae Bulleyanae As1398 neutral protease
【2014】。
Make a general survey of the studies above, there is following deficiency through analyzing:
A, after the research such as Huang Weibo uses As1398 neutral protease and papain by 1: 1 mixing in addition to enzymolysis,
Single As1398 neutral protease is all used to carry out enzymolysis.Existing many literature research confirm that each protease is only to albumen
In matter structure, aminoacid connects specific site and carries out enzymolysis, and therefore the existence of single enzyme enzymolysis is big by enzyme amount, enzymolysis time length, product
The shortcomings such as molecular weight is big.
B, protein are to be formed twisted shape structure by several (typically 2-3 bar) amino acid chain superpositions, and close structure,
The most preprocessed direct enzymolysis, protease hardly enters aminoacid and connects specific site, and therefore enzymolysis yield is relatively low.
C, protein when powdery solid be substantially do not have activated, the most just can present its enzymolysis live
Property.Therefore enzyme does not has activity to produce activity one activation process of needs to aqueous solution from solid, powdery, and this process is the shortest, whole
The process of individual enzymolysis is the shortest.Enzymolysis process one shortens, and the production efficiency of equipment just improves.
Being all to use restriction endonuclease in d, the studies above, in addition to enzymolysis efficiency is relatively low, product all has more serious bitterness.Cause
The part easily aminoacid in protein structure being contained aromatic ring and heterocycle for restriction endonuclease exposes.Therefore enzymolysis solution is made to produce more serious
Bitterness and affect mouthfeel, impact is promoted the use of.
Summary of the invention
For the problems referred to above, when the technical problem to be solved in the present invention is to provide a kind of reasonable in design, few by enzyme amount, enzymolysis
Between short, Stichopus japonicus oligopeptide production enzyme that enzymolysis yield is high and enzymolysis process.
The Stichopus japonicus oligopeptide production enzyme of the present invention and enzymolysis process, it comprises the steps of
1, on the basis of single enzyme screening, the sea including that restriction endonuclease and excision enzyme are made up of four kinds of enzymes is constituted by optimization
Ginseng enzymolysis specific complex protease；
2, in compound protease, zymoexciter is added；
3, Stichopus japonicus slurry carries out pretreatment after adjusting temperature and PH；
4, appropriate pretreating agent is added before pretreatment.
As preferably, the compound protease ratio optimized in step 1 is that papain (600,000 μ/g) accounts for 30%-60%,
Pancreatin accounts for 20%-50%, As1398 neutral protease (100,000 μ/g) and accounts for 10-40%, and food flavor enzyme (peptide ending enzyme) accounts for 5%-30%.
The consumption of compound protease is 1.0%-1.5% (total protein)；
As preferably, the zymoexciter added in step 2 has two kinds, and one is Ca2+, dosage is 1-10mmol/L；Separately
One is L-cysteine hydrochloride, and dosage is 2-20mmol/L；
As preferably, Stichopus japonicus slurry under agitation regulates PH8.0-10.5 with caustic lye of soda in step 3, is heated to 60
DEG C-80 DEG C, process 15-40min；
As preferably, slurry adds pretreating agent NaHSO before processing in step 43Or Na2SO3Or Na2S2O3, dosage is 1-
10mmol/L；
Beneficial effects of the present invention:
01, few by enzyme amount, it is the 1.0%-1.5% of Tot Prot by enzyme amount, than prior art enzyme amount 2.5%-5.0%
Fall more than 60%；
02, enzymolysis time is short, time 3-3.5h, shortens more than 40% than prior art 5-6h；
03, enzymolysis yield is high, and enzymolysis yield reaches more than 90%, improves 20% than prior art enzymolysis yield 50%-70%
Above.
04, molecular weight of product is little, application enzyme and enzymolysis process produce three batches of products send respectively state food inspection center,
Upper sea base cloud test center and the detection of test center of Southern Yangtze University, molecular weight ＜ 1000Da part accounts for before the ratio of total peptide two all
Being 100%, Southern Yangtze University is 99.58%；And major part document report does not detect molecular weight of product, open and wait report Stichopus japonicus enzyme
Hydrolysis products molecular weight ＜ 2600 content only has 1.76%, only accounts for 22% in total peptide.
05, products taste is good, the most bitter or the slightest bitterness and fishy smell.
Detailed description of the invention
Embodiment 1
Taking Stichopus japonicus appropriate, go internal organs to clean, be cut into strip, meat grinder rubs twice, if wearing into slurry then with colloid mill
More preferably.Weigh that Stichopus japonicus is broken or slurry 100g, add pure water 500ml, stir.NaHSO is added in feed liquid33mmol/L, heating
To 65 DEG C, adjust PH9.0, stir process 20min with 10%NaOH liquid.The feed liquid processed is adjusted PH8.2, is cooled to 47 DEG C ± 1
DEG C, add Ca2+3mmol/L, stirs.In feed liquid, add compound protease 0.1% (Tot Prot), stir enzymolysis 3h.By enzyme
Solve liquid PH and be adjusted to 4.5-4.6, be warming up to 65 DEG C of-70 DEG C of enzyme denaturing, cooling.95% ethanol is added dense to mixed liquor ethanol in enzymolysis solution
Degree reaches 60%-65%, precipitate polysaccharides.Standing more than 2h, centrifugal, supernatant is Stichopus japonicus oligopeptide alcoholic solution.After reclaiming ethanol,
It is adjusted to solid content 2%-5%, regular activated carbon decoloring, de-charcoal microporous filter membrane fine straining with pure water, obtains refined liquid.Use Rotary Evaporators
It is concentrated into solid content 30%-50%, obtains concentrated solution；Concentrated solution lyophilization or spray drying had both been obtained the oligomeric Gly-His-Lys of Stichopus japonicus.
Embodiment 2
Take salted sea cucumber appropriate, desalination about 6-8h in tap water flowing water, takes out.Refined immersion desalination 2-in pure water
3 times, each 2h, obtain desalination Stichopus japonicus.Desalination Stichopus japonicus is cut into granule in cutmixer, weighs Stichopus japonicus grain 10kg.Stichopus japonicus grain is existed
Slurry is worn into by colloid mill under the flowing water of pure water.With pure water regulate Stichopus japonicus grain: pure water=1: 5, stir.Under stirring
Slurry will add Na2SO34mmol/L, stirring and dissolving is uniform.Feed liquid is heated to 70 DEG C, adjusts PH9.5, stir process with NaOH liquid
30min.Feed liquid is cooled to 47 DEG C ± 1 DEG C, adjusts PH8.5 ± 0.1, add Cys 0.3mmol/L.Feed liquid add multiple
Hop protein enzyme 0.12% (Tot Prot), stirs enzymolysis 3.2h.Enzymolysis solution is adjusted PH4.5-4.6, is warming up to 70 DEG C-75 DEG C
15min enzyme denaturing.Enzymolysis solution is passed through tube centrifuge.Clear liquid passes through aperture 5000Da membrance separation, and it is oligomeric that permeate is Stichopus japonicus
Peptide liquid.Permeate takes off inorganic ions by electrodialysis plant, obtains deionization liquid.Deionization liquid adjusts about PH6.0 through conventional granulates
The de-taste of charcoal post decolouring, de-carbon granule, obtain coarse filtration liquid.Coarse filtration liquid obtains fine straining liquid through 0.1 μm-0.22 μm aperture titanium rod fine straining.Fine straining liquid
With aperture 30Da-100Da membrance concentration, obtain solid content 16%-18% liquid.This liquid is concentrated into solid content 40%-through economic benefits and social benefits again
45% concentrated solution.Concentrated solution is spray-dried, has both obtained the oligomeric Gly-His-Lys of Stichopus japonicus.
Embodiment 3
Taking unsalted dried sea cucumbers appropriate, more than steep raising 24h in pure water, without lump to Stichopus japonicus.Take out the Stichopus japonicus that steep raising is good,
Granule is cut in cutmixer.Weigh Stichopus japonicus grain 100kg.Stichopus japonicus grain is worn into slurry by colloid mill under water at stream of pure water, beats
Enter in enzymatic vessel, be initially charged the water (having water-solubility protein, polysaccharide etc. in water) of steep raising Stichopus japonicus, then adjust to material with pure water: water
=1: 5, stir.The lower slurry of stirring adds Na2S2O35mmol/L, stirring and dissolving is uniform.Feed liquid is heated to 75 DEG C, uses
NaOH liquid adjusts PH10.0, stir process 40min.Feed liquid is cooled to 48 DEG C ± 1 DEG C, adjusts PH8.6 ± 0.1.Add Ca2+
0.4mmol/L, Cys salt 0.5mmol/L.In feed liquid, add compound protease 0.15% (Tot Prot), stir enzymolysis
3.5h.Enzymolysis solution PH is adjusted to 4.5-4.6, is warming up to 75 DEG C of 15min enzyme denaturing.Enzymolysis solution is passed through tube centrifuge；Clear liquid leads to
Crossing 5000Da aperture membrance separation, permeate is Stichopus japonicus oligopeptide liquid.Permeate sloughs inorganic ions by electrodialysis plant,
Deionization liquid.Deionization liquid adjusts about PH6.0 to take off carbon granule through the de-taste of conventional granulates charcoal post decolouring, obtains coarse filtration liquid.Coarse filtration liquid is through 0.1
μm-0.22 μm titanium rod fine straining, obtains fine straining liquid.Fine straining liquid aperture 30Da-100Da membrance concentration, obtains solid content 16%-18% liquid.
This liquid is concentrated into solid content 40%-45% concentrated solution through economic benefits and social benefits again.Concentrated solution is spray-dried, obtains Stichopus japonicus oligopeptide
Powder.
The ultimate principle of the present invention and principal character and advantages of the present invention have more than been shown and described.The skill of the industry
The art personnel simply explanation it should be appreciated that the present invention is not restricted to the described embodiments, described in above-described embodiment and description
The principle of the present invention, without departing from the spirit and scope of the present invention, the present invention also has various changes and modifications, these
Changes and improvements both fall within scope of the claimed invention.Claimed scope by appending claims and
Its equivalent defines.
Claims (5)
1. Stichopus japonicus oligopeptide production enzyme and enzymolysis process, it is characterised in that it comprises the steps of
(1), on the basis of single enzyme screening, the Stichopus japonicus including that restriction endonuclease and excision enzyme are made up of four kinds of enzymes is constituted by optimization
Enzymolysis specific complex protease；
(2), in compound protease, zymoexciter is added；
(3), Stichopus japonicus slurry carries out pretreatment after adjusting temperature and PH；
(4), appropriate pretreating agent is added before pretreatment.
Stichopus japonicus oligopeptide production enzyme the most according to claim 1 and enzymolysis process, it is characterised in that described step (1)
The compound protease ratio of middle optimization is that papain accounts for 30%-60%, and pancreatin accounts for 20%-50%, As1398 neutral protein
Enzyme accounts for 10-40%, and food flavor enzyme accounts for 5%-30%；The consumption of compound protease is 1.0%-1.5%.
Stichopus japonicus oligopeptide production enzyme the most according to claim 1 and enzymolysis process, it is characterised in that described step (2)
The zymoexciter of middle addition has two kinds, and one is Ca2+, dosage is 1-10mmol/L；Another kind is L-cysteine hydrochloride, adds
Amount is 2-20mmol/L.
Stichopus japonicus oligopeptide production enzyme the most according to claim 1 and enzymolysis process, it is characterised in that described step (3)
Middle Stichopus japonicus slurry under agitation regulates PH8.0-10.5 with caustic lye of soda, is heated to 60 DEG C-80 DEG C, processes 15-40min.
Stichopus japonicus oligopeptide production enzyme the most according to claim 1 and enzymolysis process, it is characterised in that described step (4)
Middle slurry adds pretreating agent NaHSO before processing3Or Na2SO3Or Na2S2O3, dosage is 1-10mmol/L.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610654567.XA CN106282284A (en) | 2016-08-11 | 2016-08-11 | Stichopus japonicus oligopeptide production enzyme and enzymolysis process |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610654567.XA CN106282284A (en) | 2016-08-11 | 2016-08-11 | Stichopus japonicus oligopeptide production enzyme and enzymolysis process |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN106282284A true CN106282284A (en) | 2017-01-04 |
Family
ID=57669149
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201610654567.XA Pending CN106282284A (en) | 2016-08-11 | 2016-08-11 | Stichopus japonicus oligopeptide production enzyme and enzymolysis process |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN106282284A (en) |
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107212149A (en) * | 2017-06-29 | 2017-09-29 | 江南大学 | A kind of method for improving soybean protein enzyme modification reclaimed water solution yield |
| CN109757601A (en) * | 2019-03-14 | 2019-05-17 | 舜甫科技(固安)有限公司 | A kind of sea cucumber peptide and its production method |
| CN109777850A (en) * | 2019-03-25 | 2019-05-21 | 集美大学 | A kind of abalone tripe peptide and its production method and application |
| CN109797184A (en) * | 2019-03-29 | 2019-05-24 | 集美大学 | A kind of crocodile peptide and its production method |
| CN109825544A (en) * | 2019-03-27 | 2019-05-31 | 集美大学 | A kind of scallop peptide and its production method |
| CN109892661A (en) * | 2019-03-27 | 2019-06-18 | 集美大学 | A kind of pearl shell peptide and its production method |
| CN109897878A (en) * | 2019-03-29 | 2019-06-18 | 集美大学 | A kind of oyster peptide and its production method and application |
| CN109907327A (en) * | 2019-03-25 | 2019-06-21 | 集美大学 | A kind of abalone peptide and its production method |
| CN110024901A (en) * | 2019-04-30 | 2019-07-19 | 集美大学 | A kind of collagen peptide and its production method and process units and application |
| CN114958949A (en) * | 2022-05-25 | 2022-08-30 | 华南理工大学 | Maca immunoregulation protein zymolyte or peptide and preparation method and application thereof |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1334040A (en) * | 2001-08-21 | 2002-02-06 | 曲世尧 | Sea cucumber series products and production method thereof |
| CN105029513A (en) * | 2015-08-20 | 2015-11-11 | 大连润伟海参研发科技有限公司 | Method for extracting saponin, polysaccharide, peptide and melanin in wastewater obtained by boiling sea cucumbers |
| KR20150139683A (en) * | 2014-06-03 | 2015-12-14 | 재단법인 강릉과학산업진흥원 | Method for Manufacturing Fermented Sea Cucumber, and Fermented Sea Cucumber Produced Thereby |
-
2016
- 2016-08-11 CN CN201610654567.XA patent/CN106282284A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1334040A (en) * | 2001-08-21 | 2002-02-06 | 曲世尧 | Sea cucumber series products and production method thereof |
| KR20150139683A (en) * | 2014-06-03 | 2015-12-14 | 재단법인 강릉과학산업진흥원 | Method for Manufacturing Fermented Sea Cucumber, and Fermented Sea Cucumber Produced Thereby |
| CN105029513A (en) * | 2015-08-20 | 2015-11-11 | 大连润伟海参研发科技有限公司 | Method for extracting saponin, polysaccharide, peptide and melanin in wastewater obtained by boiling sea cucumbers |
Non-Patent Citations (2)
| Title |
|---|
| 汤其群: "《生物化学与分子生物学》", 30 September 2015 * |
| 郭立泉: "《酶工程》", 31 May 2011 * |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107212149A (en) * | 2017-06-29 | 2017-09-29 | 江南大学 | A kind of method for improving soybean protein enzyme modification reclaimed water solution yield |
| CN109757601A (en) * | 2019-03-14 | 2019-05-17 | 舜甫科技(固安)有限公司 | A kind of sea cucumber peptide and its production method |
| CN109777850A (en) * | 2019-03-25 | 2019-05-21 | 集美大学 | A kind of abalone tripe peptide and its production method and application |
| CN109907327A (en) * | 2019-03-25 | 2019-06-21 | 集美大学 | A kind of abalone peptide and its production method |
| CN109825544A (en) * | 2019-03-27 | 2019-05-31 | 集美大学 | A kind of scallop peptide and its production method |
| CN109892661A (en) * | 2019-03-27 | 2019-06-18 | 集美大学 | A kind of pearl shell peptide and its production method |
| CN109797184A (en) * | 2019-03-29 | 2019-05-24 | 集美大学 | A kind of crocodile peptide and its production method |
| CN109897878A (en) * | 2019-03-29 | 2019-06-18 | 集美大学 | A kind of oyster peptide and its production method and application |
| CN110024901A (en) * | 2019-04-30 | 2019-07-19 | 集美大学 | A kind of collagen peptide and its production method and process units and application |
| CN114958949A (en) * | 2022-05-25 | 2022-08-30 | 华南理工大学 | Maca immunoregulation protein zymolyte or peptide and preparation method and application thereof |
| CN114958949B (en) * | 2022-05-25 | 2023-12-22 | 华南理工大学 | Maca immunoregulatory protein hydrolysate or peptide, and preparation method and application thereof |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN106282284A (en) | Stichopus japonicus oligopeptide production enzyme and enzymolysis process | |
| CN102174627B (en) | Method for preparing rapeseed bioactive peptide | |
| WO2021142880A1 (en) | Method for producing clam active peptide | |
| CN110257459B (en) | Bird's nest small molecular peptide and instant peptide powder thereof | |
| US20220346407A1 (en) | High-clarity soybean flavor peptide, preparation method therefor, and use thereof | |
| CN105361153A (en) | Processing method of sea cucumber glycopeptides chelated calcium | |
| CN109275916A (en) | A kind of collagen polypeptide powder and preparation method thereof | |
| CN104450844A (en) | Method for extracting multiple active nutrient contents from sea cucumber processing liquid and application of method | |
| CN102550797A (en) | Production method of sea cucumber peptide extract | |
| CN103911416A (en) | Method for preparing active peptide from scallop skirts | |
| CN107668314A (en) | A kind of industrialized production pea active peptide and preparation method | |
| CN111642666A (en) | Preparation method of ginseng extract soybean peptide powder solid beverage | |
| CN106636283A (en) | Enzymolysis purification technology of mussel meat and cooking liquor | |
| CN106359839A (en) | Extraction method of oyster peptides | |
| CN109402073B (en) | Integrated extraction method of multiple bioactive components in garlic | |
| CN103882083A (en) | Method for preparing antioxidant collagen peptide | |
| CN102793138A (en) | Shellfish flavor peptide and preparation method thereof | |
| CN107753927A (en) | Chinese medicine composition of the peptide containing the membrane of a chicken's gizzard with promoting digestion and removing indigestion effect and its production and use | |
| CN105918606A (en) | Extracting method of proteins in green tea dregs | |
| JP2017513923A (en) | Method for separating and producing pearl extract from a kind of pearl | |
| CN107674905A (en) | Spirulina bioactive peptide, composition and preparation method | |
| CN106119328A (en) | A kind of high-quality shrimp oligopeptide powder, preparation method thereof of applicable industrialized production | |
| CN107583031A (en) | A kind of preparation method of albumin peptide mixer and its suppression cancer cell multiplication effect | |
| CN109293766A (en) | The method of collagen polypeptide is extracted from fish scale | |
| CN110229857B (en) | Bird's nest peptide and preparation method of depolymerized coupling enzymolysis thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20170104 |
|
| RJ01 | Rejection of invention patent application after publication |