CN105296585A - Rana chensinensis egg peptide as well as preparation method and application thereof - Google Patents
Rana chensinensis egg peptide as well as preparation method and application thereof Download PDFInfo
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Abstract
The invention belongs to the technical field of peptides and in particular relates to a rana chensinensis egg peptide as well as a preparation method and an application thereof. The preparation method comprises the following process steps: grinding and screening degreased rana chensinensis eggs; performing enzymolysis on an enzyme system combination of trypsin and papain; reacting to set time and ending the reaction; centrifuging twice, and mixing the supernatants; and performing freeze drying on the supernatant, and grinding, thereby obtaining the rana chensinensis egg peptide. The rana chensinensis egg peptide serves as a biological active peptide, can be applied to multiple aspects in medicines and diets and has high antioxidant activity, and the method provided by the invention is simple and easy to operate, and the yield of the peptide is high.
Description
Technical field
The invention belongs to polypeptide preparation technical field, be specifically related to a kind of wood frog ovum polypeptide and its preparation method and application.
Background technology
Wood frog is widely distributed in the Northeast of China, integrates medicine tonic, has very high economic worth, and is day by day subject to the attention of domestic and international production, processing and circulation enterprise.Wood frog ovum has very high nutritive value, and there is different physiological roles, can be applicable to pharmacy and protective foods, degreasing (supercritical extraction) dried Woodfrog egg protein matter content can reach more than 80%, and its amino acid classes is complete, 9 kinds of indispensable amino acids containing needed by human body, the ratio (E/T) of indispensable amino acid and total amino acid is up to 50%, and rich trace elements is the healthy food material of natural high-quality.
Biologically active peptides (bioactivepeptides) to be made up of with difference 20 seed amino acids and to be formed with arrangement mode, has amino acid and the incomparable physiological function of protein.The osmotic pressure of biologically active peptides is lower than total free aminoacids, and its specific absorption is high, and sensitization is low, and security is high.In addition, because the diversity of its structure and complicacy make it have multiple biological activity, large quantifier elimination shows, they also have potential hypotensive, and reducing blood-fat is anti-oxidant, anti-ageing, antiviral, antibacterial, anticancer, growth promoting effects, calm, reduce cholesterol, promote mineral absorption, improve substance metabolism, the various functions such as enhancing body immunological competence, these functions are all much that its crude protein and single amino acid are unexistent.Now research shows, the inhibiting rate of multipair OH and DPPH prepared by enzymolysis wood frog ovum reaches 80.91% and 70.45% respectively, illustrates that it has higher anti-oxidant activity.Wood frog ovum anti-oxidation peptide has anti-oxidant, to protect the physiological functions such as microbial film, scavenging free radicals, detoxication and toxicant eliminating function biologically active peptides, is a class non-enzyme free-radical scavengers.Because it is without any side effects, security is high, oxidation-resistance advantages of higher, can be added in ordinary meal as natural antioxidants.
But for a long time, woodfrog egg oil is the main products of wood frog ovum, and the wood frog ovum after degreasing is regarded as processing byproduct always, it develops and is still in the blank stage, causes the waste of high-quality animal protein resource.Along with the development of modern biotechnology, suitability for industrialized production has started to utilize enzymatic hydrolysis to improve the functional property of protein, and obtained bioactive peptide can be used as the base-material of food or dietary supplements.And research shows, food endogenous binding protein matter is after Digestive tract enzymically hydrolyse, and mainly absorbed with the form of little peptide, its body absorption rate specific ionization amino acid is higher.Peptide, compared with protein, has better physico-chemical property, processing characteristics and physiological function.Therefore, developing Woodfrog egg protein, to prepare polypeptide significant for the economic benefit improving protein resource utilization ratio and wood frog industry.
Summary of the invention
In order to solve the problem that degreasing Woodfrog egg protein in prior art not yet carries out fully developing, the invention provides a kind of wood frog ovum polypeptide and its preparation method and application, obtained wood frog ovum polypeptide can be used as natural antioxidants and adds in ordinary meal, promotes health.
The present invention is achieved in that according to an aspect of the present invention, provides a kind of preparation method of wood frog ovum polypeptide, comprises the steps:
1) crush and screen, degreaser drying wood frog ovum is pulverized and sieved;
2) enzymolysis, by step 1) in preparation wood frog ovum powder thin up, heat and keep constant temperature, regulate pH, add trypsinase, papoid enzyme system combination carry out enzyme digestion reaction degrade wood frog ovum;
3) go out enzyme, reacts to setting-up time, regulates pH, water-bath termination reaction;
4) two times centrifugal, merges supernatant liquor;
5) by supernatant liquor lyophilize, obtained wood frog ovum polypeptides freeze-dry powder, is ground to uniform powder, obtained described wood frog ovum polypeptide.
Further, step 1) in by degreaser drying wood frog ovum pulverize after cross 60 mesh sieves.
Further, step 2) in add water and make wood frog ovum powder dilute 2.5-3.5 doubly, maintenance thermostat temperature is 25-35 DEG C, is 6 by lmol/LNaOH solution or lmol/LHCl solution regulation system pH value.
Further, step 2) in trypsinase, papoid enzyme addition of living be 10400u/g material, trypsinase: the enzyme of papoid is lived than being 1.13, and concentration of substrate 10%, hydrolysis temperature 45-55 DEG C, pH7.70, the reaction times is 3.5-4.5h.
Further, step 3) in be 7.0 by lmol/LNaOH solution or lmol/LHCl solution adjust ph, bath temperature is 85-95 DEG C, water bath time 8-12min.
Further, step 4) in centrifuging temperature 4 DEG C, rotating speed be 8000r/min, the time is 15min, and centrifugal rear distilled water wash precipitation carries out secondary centrifuging first.
According to another one aspect of the present invention, additionally provide a kind of wood frog ovum polypeptide prepared according to the method described above.
Present invention also offers above-mentioned wood frog ovum polypeptide as the application of natural antioxidants in medicine, ordinary meal.
Compared with prior art, the invention has the advantages that, wood frog ovum is utilized to prepare wood frog ovum polypeptide, by the wood frog ovum recycling after degreasing, the wood frog ovum polypeptide of gained, as a kind of biologically active peptides, can be applicable to the many aspects such as medicine, meals, has higher anti-oxidant activity, and method provided by the invention is simple to operation, and polypeptide yield is high.
Accompanying drawing explanation
Below in conjunction with drawings and the embodiments, the present invention is further detailed explanation:
Fig. 1 is the typical curve that BCA method measures content of peptides;
Fig. 2 is wood frog ovum polypeptide fourier infrared scanning spectrogram prepared by the present invention;
Fig. 3 is wood frog ovum polypeptide amino acid analysis of spectra prepared by the present invention.
Embodiment
Clearly understand to make object of the present invention, technical scheme and advantage, below in conjunction with embodiment and accompanying drawing, the present invention is further elaborated, is to be understood that, specific embodiment described herein only for explaining the present invention, is not intended to limit the present invention.
Containing a large amount of protein in wood frog ovum after degreasing, application Micro-kjoldahl method (with reference to GB/T5009.5-2003), determining degreaser drying Woodfrog egg protein content is 81.36%, but up to the present, woodfrog egg oil remains the main products of wood frog ovum, after degreasing, in wood frog ovum, a large amount of albumen is thrown away and is extracted fully and utilize, in order to solve in prior art for the blank that degreasing Woodfrog egg protein utilizes, the invention provides a kind of wood frog ovum polypeptide and its preparation method and application, by pulverizing and sieving → enzymolysis → termination reaction → centrifugal → lyophilize obtains described wood frog ovum polypeptide powder, medicine can be applied in, the many aspects such as meals.
Embodiment 1
Utilize method provided by the invention to prepare wood frog ovum polypeptide, used material and instrument are commercially available.
1) crush and screen, 13g degreaser drying wood frog ovum Portable high speed medicinal herb grinder is pulverized, crosses 60 mesh sieves;
2) enzymolysis, by step 1) in preparation wood frog ovum powder adding distil water dilute 2.5 times, be heated to 25 DEG C and keep constant temperature, be 6 by lmol/LNaOH solution or lmol/LHCl solution regulation system pH value, add trypsinase, papoid, trypsinase according to enzyme addition 10400u/g material of living: the enzyme of papoid is lived than being 1.13, concentration of substrate 10%, hydrolysis temperature 45 DEG C, pH7.70, the reaction times is 3.5h;
3) go out enzyme, reacts to 3.5h, is 7.0 by lmol/LNaOH solution or lmol/LHCl solution adjust ph, water-bath termination reaction, and bath temperature is 85 DEG C, water bath time 8min;
4) two times centrifugal, merge supernatant liquor, centrifuging temperature 4 DEG C, rotating speed are 8000r/min, and the time is 15min, and centrifugal rear distilled water wash precipitation carries out secondary centrifuging first;
5) by supernatant liquor lyophilize, obtained wood frog ovum polypeptides freeze-dry powder, is ground to uniform powder, obtained described wood frog ovum polypeptide.
Embodiment 2
1) crush and screen, 13g degreaser drying wood frog ovum Portable high speed medicinal herb grinder is pulverized, crosses 60 mesh sieves;
2) enzymolysis, by step 1) in preparation wood frog ovum powder adding distil water dilute 3 times, be heated to 30 DEG C and keep constant temperature, be 6 by lmol/LNaOH solution or lmol/LHCl solution regulation system pH value, add trypsinase, papoid, trypsinase according to enzyme addition 10400u/g material of living: the enzyme of papoid is lived than being 1.13, concentration of substrate 10%, hydrolysis temperature 48.8 DEG C, pH7.70, the reaction times is 4h;
3) go out enzyme, reacts to 4h, is 7.0 by lmol/LNaOH solution or lmol/LHCl solution adjust ph, water-bath termination reaction, and bath temperature is 90 DEG C, water bath time 10min;
4) two times centrifugal, merge supernatant liquor, centrifuging temperature 4 DEG C, rotating speed are 8000r/min, and the time is 15min, and centrifugal rear distilled water wash precipitation carries out secondary centrifuging first;
5) by supernatant liquor lyophilize, obtained wood frog ovum polypeptides freeze-dry powder, is ground to uniform powder, obtained described wood frog ovum polypeptide.
Embodiment 3
1) crush and screen, 13g degreaser drying wood frog ovum Portable high speed medicinal herb grinder is pulverized, crosses 60 mesh sieves;
2) enzymolysis, by step 1) in preparation wood frog ovum powder adding distil water dilute 3.5 times, be heated to 35 DEG C and keep constant temperature, be 6 by lmol/LNaOH solution or lmol/LHCl solution regulation system pH value, add trypsinase, papoid, trypsinase according to enzyme addition 10400u/g material of living: the enzyme of papoid is lived than being 1.13, concentration of substrate 10%, hydrolysis temperature 55 DEG C, pH7.70, the reaction times is 4.5h;
3) go out enzyme, reacts to 4.5h, is 7.0 by lmol/LNaOH solution or lmol/LHCl solution adjust ph, water-bath termination reaction, and bath temperature is 95 DEG C, water bath time 12min;
4) two times centrifugal, merge supernatant liquor, centrifuging temperature 4 DEG C, rotating speed are 8000r/min, and the time is 15min, and centrifugal rear distilled water wash precipitation carries out secondary centrifuging first;
5) by supernatant liquor lyophilize, obtained wood frog ovum polypeptides freeze-dry powder, is ground to uniform powder, obtained described wood frog ovum polypeptide.
Embodiment 4
The mensuration of content of peptides
Adopt BCA method (protein concn linear detection range is 100 ~ 2000 μ g/mL), measuring principle:
Protein (peptide bond)+Cu
2+→ Cu
l+-the tetramer
Cu
l++ 2BCA → BCA-Cu
l+mixture
The BCA-Cu of purple
l+mixture has maximum absorption band at 562nm place.
(1) preparation of working solution:
A liquid: by BCA2g, anhydrous Na CO
34g, NaOH0.8g, NaHCO
31.9g, Seignette salt 0.46g mixes and is dissolved in distilled water, is settled to 200mL.
B liquid: 4% copper sulfate
The A liquid of 50 volumes is mixed with the B liquid of 1 volume, is standard operation reagent after resolution of precipitate, in peak green.This working solution is at room temperature stablized, and the same day uses.
(2) standard protein solution preparation:
Prepare bovine serum albumin (BSA) standardized solution with distilled water, 0.9% physiological saline, PBS, BSA concentration of standard solution is respectively 2000,1500,1000,750,500,250,100 μ g/mL.
(3) protein determination
0.1mL is treated sample measuring liquid mixes with 2mL standard working solution, water-bath 30min at 37 DEG C.To be cooled to room temperature, light absorption value (A) is measured under 562nm, drawing standard curve, with reference to figure 1, calculating according to typical curve the wood frog ovum peptide concentration mean value that embodiment 1,2,3 utilizes the method to extract is 932 μ g/mL, and utilizing this mean value to converse contained protein mass per-cent in wood frog ovum polypeptides freeze-dry powder is 59.42%.
Embodiment 5
The analysis of wood frog ovum polypeptide structure
Infrared scan is analyzed
Dry for 100-150mg KBr and wood frog ovum polypeptides freeze-dry powder are put in mortar with the mass ratio of 200:1, grind to form uniform powder, dress sample, compressing tablet, sample chamber put into by sample, and adopt Fourier infrared spectrograph to Sample Scan within the scope of 400/cm ~ 4000/cm, resolving power is 4/cm.
Scanning result is with reference to figure 2, known, and acid amides A comes across 3424.37cm
-1near, be the absorption peak of N-H symmetrical stretching vibration, illustrate that hydrogen bond exists; Acid amides B comes across 2990.13cm
-1near, be N-H antisymmetric stretching vibration, CH
2, the stretching vibration of CH group absorption peak; Acid amides I appears at 1682.64cm
-1, it is relevant with secondary protein structure, is the absorption peak of the stretching vibration of C=O, and due to mesomeric effect, the C=O absorption frequency of peptide bond is lower than aldehyde ketone, and (C=O of aldehyde ketone and carboxylic acid absorbs and is all not less than 1700cm
-1), this illustrates that wood frog ovum polypeptide exists secondary structure; Acid amides II is at 1583.33cm
-1near, acid amides III is at 1228.32cm
-1near, represent the flexural vibration of N-H and the stretching vibration of C-H respectively, acid amides II, acid amides III is relevant with spirane structure.
Acid amides II absorbs by force with one group, and this represents that N-H exists with transconfiguration form relative to C=O, and 1425.75cm
-1the form that neighbouring appearance one group is cis-configuration compared with weak absorbing exists, and trans absorption is far better than cis and absorbs, acid amides III (1228.32cm
-1near) there is strong absorption, these illustrate that polypeptide chain exists spirane structure.Therefore, fourier infrared scanning demonstrate this test prepare wood frog ovum polypeptide save than more complete α-helixstructure.
Amino acid composition analysis
Through automatic analyzer for amino acids, amino acid analysis spectrogram is shown in Fig. 3 (X-coordinate is retention time, and ordinate zou is response intensity).Through calculating, amino acid whose kind and content in known wood frog ovum polypeptide, see the following form:
As seen from the above table, containing 17 kinds of nitrogen base acid in wood frog ovum polypeptide prepared by method provided by the invention, wherein containing 7 kinds of essential amino acids.Isoleucine (Ile), L-Ala (Ala), glycine (Gly), α-amino-isovaleric acid (Val) content higher (in acid hydrolysis, tryptophane is almost destroyed).
Claims (8)
1. the preparation method of wood frog ovum polypeptide, is characterized in that, comprises the steps:
1) crush and screen, degreaser drying wood frog ovum is pulverized and sieved;
2) enzymolysis, by step 1) in preparation wood frog ovum powder thin up, heat and keep constant temperature, regulate pH, add trypsinase, papoid enzyme system combination carry out enzyme digestion reaction degrade wood frog ovum;
3) go out enzyme, reacts to setting-up time, regulates pH, water-bath termination reaction;
4) two times centrifugal, merges supernatant liquor;
5) by supernatant liquor lyophilize, obtained wood frog ovum polypeptides freeze-dry powder, is ground to uniform powder, obtained described wood frog ovum polypeptide.
2., according to the preparation method of wood frog ovum polypeptide according to claim 1, it is characterized in that, step 1) in by degreaser drying wood frog ovum pulverize after cross 60 mesh sieves.
3. according to the preparation method of wood frog ovum polypeptide according to claim 1, it is characterized in that, step 2) in add water and make described wood frog ovum powder dilute 2.5-3.5 doubly, maintenance thermostat temperature is 25-35 DEG C, is 6 by lmol/LNaOH solution or lmol/LHCl solution regulation system pH value.
4. according to the preparation method of wood frog ovum polypeptide according to claim 1, it is characterized in that, step 2) described in trypsinase, papoid enzyme live addition be 10400u/g material, trypsinase: the enzyme of papoid is lived than being 1.13, concentration of substrate 10%, hydrolysis temperature 45-55 DEG C, pH7.70, the reaction times is 3.5-4.5h.
5., according to the preparation method of wood frog ovum polypeptide according to claim 1, it is characterized in that, step 3) in be 7.0 by lmol/LNaOH solution or lmol/LHCl solution adjust ph, bath temperature is 85-95 DEG C, water bath time 8-12min.
6., according to the preparation method of wood frog ovum polypeptide according to claim 1, it is characterized in that, step 4) in centrifuging temperature 4 DEG C, rotating speed be 8000r/min, the time is 15min, and centrifugal rear distilled water wash precipitation carries out secondary centrifuging first.
7. according to wood frog ovum polypeptide prepared by the arbitrary described method of claim 1 ~ 6.
8. according to wood frog ovum polypeptide according to claim 7 as natural antioxidants in medicine, application in ordinary meal.
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106983853A (en) * | 2017-03-05 | 2017-07-28 | 赵德润 | A kind of wood frog's fallopian tube active peptide and preparation method thereof |
| CN107951019A (en) * | 2017-12-21 | 2018-04-24 | 杭州妇帮医疗科技有限公司 | A kind of functional food for improving female infertility and preparation method thereof |
| CN108813633A (en) * | 2018-05-16 | 2018-11-16 | 林万君 | Wood frog ovum Gly-His-Lys |
| CN110438185A (en) * | 2019-07-31 | 2019-11-12 | 杭州妇帮医疗科技有限公司 | A method of extracting the polypeptide moiety in wood frog ovum |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101392283A (en) * | 2008-11-12 | 2009-03-25 | 通化市林蛙研究所 | Enzymatic hydrolysis method for extracting high F value oligopeptide mixture from rana chensinensis egg oil |
| CN101664192A (en) * | 2009-09-11 | 2010-03-10 | 黑龙江大通生物技术有限公司 | Preparation method of rana chensinensis frogspawn calcium amino acid chelated food |
-
2015
- 2015-11-04 CN CN201510741558.XA patent/CN105296585A/en active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101392283A (en) * | 2008-11-12 | 2009-03-25 | 通化市林蛙研究所 | Enzymatic hydrolysis method for extracting high F value oligopeptide mixture from rana chensinensis egg oil |
| CN101664192A (en) * | 2009-09-11 | 2010-03-10 | 黑龙江大通生物技术有限公司 | Preparation method of rana chensinensis frogspawn calcium amino acid chelated food |
Non-Patent Citations (3)
| Title |
|---|
| R.M.WYNN编，周苏文等译: "《子宫生物学》", 28 February 1982, 人民卫生出版社 * |
| 任发政等: "《乳蛋白及多肽的结构与功能》", 31 January 2015, 中国农业科学技术出版社 * |
| 吕集等: "林蛙卵提取高F值低聚肽混合物的酶解方法", 《食品研究与开发》 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106983853A (en) * | 2017-03-05 | 2017-07-28 | 赵德润 | A kind of wood frog's fallopian tube active peptide and preparation method thereof |
| CN107951019A (en) * | 2017-12-21 | 2018-04-24 | 杭州妇帮医疗科技有限公司 | A kind of functional food for improving female infertility and preparation method thereof |
| CN108813633A (en) * | 2018-05-16 | 2018-11-16 | 林万君 | Wood frog ovum Gly-His-Lys |
| CN110438185A (en) * | 2019-07-31 | 2019-11-12 | 杭州妇帮医疗科技有限公司 | A method of extracting the polypeptide moiety in wood frog ovum |
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