CN101845472A - Method for preparing scale collagen antioxidant peptides by using no-feed supplement enzymolysis-membrane separation coupling technology - Google Patents
Method for preparing scale collagen antioxidant peptides by using no-feed supplement enzymolysis-membrane separation coupling technology Download PDFInfo
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Abstract
The invention discloses a method for preparing antioxidant peptides by using a no-feed supplement enzymolysis-membrane separation coupling technology and relates to a method for preparing scale collagen antioxidant peptides by using the no-feed supplement enzymolysis-membrane separation coupling technology, belonging to the technical field of leftover deep processing of aquatic products. The method comprises the following steps of: preparing raw material solutions with a certain substrate concentration, filling in a reaction kettle and then regulating the pH and the reaction temperature of reacted solutions; and circulating the raw material solutions several minutes under the certain rotation speed of a circulating pump, then adding protease, and carrying out continuous enzymolysis-membrane separation coupling reaction under constant-speed circulation or firstly high-speed and then low-speed variable-speed circulation to collect permeated solutions which are antioxidant peptide solutions. The method for preparing the scale collagen antioxidant peptides by applying the enzymolysis-membrane separation coupling technology overcomes the shortages existing in the traditional method with divided operations of enzymolysis and membrane separation, also overcomes the shortages existing in constant-speed circulation due to variable-speed circulation and obviously improves enzymolysis reaction efficiency and the activities of products.
Description
Technical field
The present invention relates to no-feed supplement enzymolysis-membrane sepn coupling prepares the method for fish scale collagen anti-oxidation peptide, belongs to fishery products tankage deep process technology field.
Background technology
China is an aquatic products big country, produces a large amount of tankage in the product that cures fish, and its total amount accounts for the 50%-70% of the total mass that cures fish, and wherein about 5% is fish scale.Yet, be subjected to the restriction of technology and traditional concept, in long period of time, fish scale is not fully utilized, and is thrown away but be used as rubbish.According to estimates, the waste total amount that I cross annual fish just reaches more than 2,000,000 tons, and wherein fish scale is about 100,000 tons.Existing studies show that: fish scale can be processed into collagen protein, gelatin etc. and be applied to edible cosmetic product industry, the peptide that the fish scale collagen hydrolysis is obtained, compare with collagen protein, molecular weight is relatively low, the polypeptide that the former proteolysis of existing technique table gelatin obtains, have the elevation of blood pressure of inhibition, suppress the platelet aggregation isoreactivity, but do not see the report of using it for anti-oxidant activity as yet.
Traditional method for preparing scale collagen polypeptide, acid, enzyme or the alkali of adopting extract more, and required time is mostly about 12-72 hour, and the degree of hydrolysis that obtains also has only about 20%-50%, this method process for processing is consuming time and need a large amount of acid, alkali, and sewage load is very big.With enzyme process preparation can be above-mentioned the part deficiency, but facts have proved that adopts traditional zymolysis technique, problems such as product retarding effect and polypeptide excessive degradation can appear in the carrying out along with reacting.In recent years a large amount of studies have shown that, enzymolysis-film separation coupling technique can overcome traditional zymolysis technique and have deficiency, significantly improves the activity of enzyme digestion reaction efficient and product.Do not see the report that enzymolysis-film separation coupling technique is applied to the preparation of fish scale collagen anti-oxidation peptide as yet.
Summary of the invention
The objective of the invention is in order to overcome above-mentioned deficiency of the prior art, disclosing no-feed supplement enzymolysis-membrane sepn coupling a kind of prepares the method for polypeptide, it is characterized in that carrying out according to following step, dispose the material solution of certain concentration of substrate, the reactor of packing into, conditioned reaction liquid pH and temperature of reaction, make material solution cycle number minute under certain recycle pump rotating speed earlier, add proteolytic enzyme then, under constant speed circulation or " elder generation is the speed change circulation of back low speed at a high speed ", carry out continuous enzymolysis-membrane sepn coupling reaction again, collect through liquid and promptly get polypeptide solution.
Under the situation of no-feed supplement, the method that the coupling of above-mentioned no-feed supplement enzymolysis-membrane sepn prepare polypeptide is applied to the preparation of fish scale collagen anti-oxidation peptide, and continuous enzymolysis-membrane sepn is coupled and prepares the method for fish scale collagen anti-oxidation peptide.
Technical scheme of the present invention is carried out according to following step: the certain rotating speed cycle number of fish scale collagen solution → conditioned reaction liquid pH, the temperature of reaction → ultrafiltrate pump of certain concentration of substrate minute → enzyme-added → carry out constant speed circulation or speed change circulation enzymolysis-membrane sepn coupling reaction → collections are through liquid → mensuration substrate protein transformation efficiency.
Wherein said fish scale collagen solution concentration of substrate mass ratio is 0.5%-4%;
Wherein said proteolytic enzyme is Alcalase, and conditioned reaction liquid pH and temperature of reaction are 45 ℃-60 ℃ of the peak enzymolysis-ability temperature of the Alcalase that recommends, and reaction solution is that pH is 8.5-9.5;
Wherein said enzyme concentration is the 0.5%-4% that accounts for the fish scale collagen mass ratio;
Wherein said enzyme-added before material solution cycling time be 5min;
Wherein said reaction times 10-60min;
Wherein said constant speed circulation, its speed of circulation is 80-120r/min;
Wherein said " earlier at a high speed, the circulation of the speed change of back low speed " promptly earlier reacts 20min under the recycle pump rotating speed of 150r/min, after the rotating speed of recycle pump turned down to 100r/min react 6min, carry out speed change circulation enzymolysis-membrane sepn coupling reaction;
Adopting molecular weight cut-off in the ultra-filtration process among the present invention is the Mierocrystalline cellulose flat sheet membrane of 3kDa-10kDa, the Mierocrystalline cellulose flat sheet membrane of preferred 3kDa.
The present invention uses no-feed supplement speed change circulation enzymolysis-film separation coupling technique and prepares the fish scale collagen anti-oxidation peptide, overcomes traditional zymolysis technique and has deficiency, significantly improves the activity of enzyme digestion reaction efficient and product.
Description of drawings
Fig. 1 is continuous enzyme membrane coupling reaction device synoptic diagram for the no-feed supplement speed change circulates, wherein the 1-thermostat water bath; The 2-enzymolysis reactor; The 3-precision acidity meter; The 4-hyperfiltration membrane assembly; 5-goes out the peptide valve; The 6-recycle pump;
Fig. 2 is the graph of a relation of the molecular weight cut-off of the clearance rate of DPPH free radical of enzymolysis product and Mierocrystalline cellulose flat sheet membrane;
Fig. 3 for the no-feed supplement speed change circulates during continuous enzyme membrane coupling reaction the different recycle pump following times of rotating speed (t) to the influence of albumen transformation efficiency (X).
Embodiment
With the example that is prepared as of fish scale collagen anti-oxidation peptide, introduce continuous enzymolysis of the present invention-membrane sepn coupling and prepare the method for fish scale collagen anti-oxidation peptide below.Weigh preparation method's of the present invention technique effect by measuring the fish scale collagen transformation efficiency among the present invention, wherein the mensuration of protein content adopts Kjeldahl determination (GB/T5009.3-2003).
The albumen transformation efficiency accounts for protein content percentage calculation in the stock liquid with membrane filtration through protein content in the liquid:
In the formula: X-albumen transformation efficiency, %; C
0-stock liquid protein content, mg/mL; V
0-stock liquid cumulative volume, mL; C
1-through the white content of liquid eggs, mg/mL; V
1-through liquid cumulative volume, mL.
The clearance rate of DPPH free radical is estimated the anti-oxidant activity of enzymolysis product by measuring enzymolysis product among the present invention.Enzymolysis product goes out and is diluted to unified concentration behind the enzyme, measures the clearance rate of DPPH free radical.
Measuring method: the enzymolysis supernatant liquor is diluted to different concentration gradients, the enzymolysis supernatant liquor of getting the 2mL different concns respectively is in test tube, adding 2mL concentration is the DPPH solution of 0.04mg/ml, mix, behind the reaction 20min, in the centrifugal 10min of 3500rpm, getting supernatant liquor is A at 517nm place its light absorption value of survey
iRespectively get the above-mentioned concentration supernatant soln of 2mL in test tube in addition, add dehydrated alcohol 2mL respectively, behind the reaction 20min,, get supernatant liquor and be designated as A at 517nm place its light absorption value of survey in 3500rpm centrifugation 10min
jReact as reference with 2mL 0.04mg/mL DPPH and 2mL dehydrated alcohol, its light absorption value is designated as A
0
E
(DPPH)＝[1-(A
i-A
j)/A
0]×100％
In the formula: E
(DPPH)-enzymolysis supernatant liquor is to the clearance rate (%) of DPPH free radical;
A
0-2mL DPPH solution adds the light absorption value of 2mL dehydrated alcohol;
A
i-2mL DPPH solution adds the light absorption value of 2mL enzymolysis supernatant;
A
j-2mL dehydrated alcohol adds the light absorption value of 2mL enzymolysis supernatant liquor.
EC
50Calculating: EC
50The DPPH clearance rate that is enzymolysis product reaches 50% o'clock concentration.At first diluted sample is become a series of concentration, measure the clearance rate of each concentration sample, draw the relation curve of clearance rate and concentration, on curve, find the EC of sample DPPH
50Value.
Determining of the molecular weight cut-off of Mierocrystalline cellulose flat sheet membrane: among the present invention at first the clearance rate of the DPPH free radical by measuring enzymolysis product determine the molecular weight cut-off of Mierocrystalline cellulose flat sheet membrane, test is carried out according to following step, concentration of substrate is 50 ℃ of 2% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 120r/min of reaction solution pH8.5 → ultrafiltrate pump, the Mierocrystalline cellulose flat sheet membrane that circulation 5min → adding accounts for the protease A lcalase → enzymolysis 40min → employing PSPP of substrate 0.5% is carried out ultrafiltration → collection and is seen through liquid → mensuration product to the clearance rate of DPPH and calculate EC
50Value.The result takes all factors into consideration clearance rate and the EC of enzymolysis product to DPPH as shown in Figure 2
50Value, preferred molecular weight cut-off is that the Mierocrystalline cellulose flat sheet membrane of the 3kDa product after to enzymolysis carries out ultrafiltration among the present invention.
Embodiment 1
Present embodiment carries out according to following step, and concentration of substrate is that fish scale collagen solution → 50 ℃ of conditioned reaction liquid temperature of reaction of 2%, reaction solution pH8.5 → ultrafiltrate pump account in the 5min → adding that circulates under the rotating speed 120r/min under protease A lcalase → 120r/min constant speed circulation of substrate 0.5% and carry out " enzymolysis-membrane sepn coupling reaction " 40min → collections through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Present embodiment carries out according to following step, concentration of substrate is 55 ℃ of 2% fish scale collagen solution → conditioned reaction liquid temperature of reaction, and reaction solution pH9.0 → ultrafiltrate pump accounts in the 5min → adding that circulates under the rotating speed 100r/min under protease A lcalase → 100r/min constant speed circulation of substrate 1.5% and carries out " enzymolysis-membrane sepn coupling reaction " 30min → collections through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Embodiment 3
Present embodiment carries out according to following step, concentration of substrate is 60 ℃ of 2% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 80r/min of reaction solution pH9.5 → ultrafiltrate pump, circulation 5min → adding accounts for the protease A lcalase of substrate 1% → 80r/min constant speed circulation and carries out " enzymolysis-membrane sepn coupling reaction " 50min → collection down through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Present embodiment carries out according to following step, concentration of substrate is 55 ℃ of 4% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 80r/min of reaction solution pH8.5 → ultrafiltrate pump, circulation 5min → adding accounts for the protease A lcalase of substrate 1% → 80r/min constant speed circulation and carries out " enzymolysis-membrane sepn coupling reaction " 50min → collection down through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Present embodiment carries out according to following step, concentration of substrate is 55 ℃ of 2% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 120r/min of reaction solution pH9.0 → ultrafiltrate pump, circulation 5min → adding accounts for the protease A lcalase of substrate 0.5% → 120r/min constant speed circulation and carries out " enzymolysis-membrane sepn coupling reaction " 40min → collection down through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Embodiment 6
Present embodiment carries out according to following step, concentration of substrate is 50 ℃ of 3% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 80r/min of reaction solution pH9.5 → ultrafiltrate pump, circulation 5min → adding accounts for the protease A lcalase of substrate 1.5% → 80r/min constant speed circulation and carries out " enzymolysis-membrane sepn coupling reaction " 40min → collection down through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Embodiment 7
Present embodiment carries out according to following step, concentration of substrate is 50 ℃ of 3% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 100r/min of reaction solution pH9.0 → ultrafiltrate pump, circulation 5min → adding accounts for the protease A lcalase of substrate 1.5% → 100r/min constant speed circulation and carries out " enzymolysis-membrane sepn coupling reaction " 50min → collection down through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Find the significant effects that the recycle pump rotating speed has the albumen transformation efficiency in the present invention's research, by of the influence of research recycle pump rotating speed, determine best techniques parameter of the present invention in the present embodiment the albumen transformation efficiency.
Enzyme membrane coupling reaction condition: enzyme concentration 1.5%, reaction solution pH9.0,55 ℃ of temperature of reaction, concentration of substrate 3%.The time dependent curve of albumen transformation efficiency is as shown below under the different recycle pump rotating speeds.
By shown in Figure 3, when the rotating speed of recycle pump is high, increase along with the time, proteinic transformation efficiency rises rapidly, but reaches the point of inversion of steady stage very soon, and its reason should be a Rapid Cycle, help on the one hand the micromolecule polypeptide that enzymolysis comes out and in time discharge reactive system, the reinforcing mass transfer effect of liquid circulation helps promoting the contact of enzyme-to-substrate on the other hand, but substrate becomes not enough behind the 20min, and circulation fast becomes on the contrary and reduces effective contact of enzyme-to-substrate.From this curve of 100r/min as can be seen, for lower rotating speed, after point of inversion 30min, proteinic transformation efficiency also rises with certain speed, therefore explanation reaction relatively low speed of circulation of later stage under the situation that does not influence the polypeptide discharge, helps promoting proteinic enzymolysis.Therefore for the operating mode of no-feed supplement among the present invention, preferably take earlier the speed change cyclic policy of back low speed at a high speed, should help improving proteinic transformation efficiency.
Present embodiment has been taked recycle pump circulation at a high speed earlier, low speed round-robin speed change cyclic policy again, carry out according to following step, concentration of substrate is 55 ℃ of 3% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 100r/min of reaction solution pH9.0 → ultrafiltrate pump, circulation 5min → adding accounts for the rotating speed 150r/min reaction 20min of the protease A lcalase → first recycle pump of substrate 1.5%, the rotating speed of recycle pump is turned down to the circulation of 100r/min reaction 6min speed change again and is carried out " enzymolysis-membrane sepn coupling reaction " 26min → collection through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase 2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Present embodiment carries out according to following step, concentration of substrate is 55 ℃ of 3% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 100r/min of reaction solution pH9.0 → ultrafiltrate pump, circulation 5min → adding accounts for the rotating speed 150r/min reaction 20min of the protease A lcalase → first recycle pump of substrate 1.5%, the rotating speed of recycle pump is turned down to the circulation of 100r/min reaction 6min speed change again and is carried out " enzymolysis-membrane sepn coupling reaction " 26min → collection through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Present embodiment carries out according to following step, concentration of substrate is 60 ℃ of 4% fish scale collagen solution → conditioned reaction liquid temperature of reaction, the rotating speed 120r/min of reaction solution pH9.5 → ultrafiltrate pump, circulation 5min → adding accounts for the rotating speed 150r/min reaction 20min of the protease A lcalase → first recycle pump of substrate 1.5%, the rotating speed of recycle pump is turned down to the circulation of 100r/min reaction 6min speed change again and is carried out " enzymolysis-membrane sepn coupling reaction " 26min → collection through liquid → mensuration substrate protein transformation efficiency.(wherein membrane sepn employing molecular weight cut-off is the Mierocrystalline cellulose flat sheet membrane of 3kDa; Fish scale collagen, the commercially available prod; Alcalase2.4L, letter (China) Bioisystech Co., Ltd of Novi.)
Claims (5)
1. no-feed supplement enzymolysis-membrane sepn coupling prepares the method for polypeptide, it is characterized in that carrying out according to following step, dispose the material solution of certain concentration of substrate, the reactor of packing into, conditioned reaction liquid pH and temperature of reaction make material solution cycle number minute under certain recycle pump rotating speed earlier, add proteolytic enzyme then, under constant speed circulation or " elder generation is the speed change circulation of back low speed at a high speed ", carry out continuous enzymolysis-membrane sepn coupling reaction again, collect through liquid and promptly get anti-oxidation peptide solution.
2. no-feed supplement enzymolysis according to claim 1-membrane sepn coupling prepares the method for polypeptide, it is characterized in that described raw material is a fish scale collagen, and the product for preparing is the fish scale collagen anti-oxidation peptide.
3. no-feed supplement enzymolysis according to claim 2-membrane sepn coupling prepares the method for fish scale collagen anti-oxidation peptide, it is characterized in that wherein said fish scale collagen solution concentration of substrate mass ratio is 0.5%-4%; Wherein said proteolytic enzyme is Alcalase, and conditioned reaction liquid pH and temperature of reaction are that 8.5-9.5, temperature are 45 ℃-60 ℃ for the peak enzymolysis-ability reaction solution pH of the Alcalase of recommendation; Wherein said enzyme concentration is the 0.5%-4% that accounts for the fish scale collagen mass ratio; Wherein said enzyme-added before material solution cycling time be 5min; The wherein said reaction times is 10-60min; Wherein said constant speed circulation is and carries out constant speed circulation enzymolysis-membrane sepn coupling reaction under speed of circulation 80-120r/min; Wherein adopting molecular weight cut-off in the ultra-filtration process is the Mierocrystalline cellulose flat sheet membrane of 3kDa-10kDa.
4. no-feed supplement enzymolysis according to claim 2-membrane sepn coupling prepares the method for fish scale collagen anti-oxidation peptide, it is characterized in that wherein said fish scale collagen solution concentration of substrate mass ratio is 0.5%-4%; Wherein said proteolytic enzyme is Alcalase, and conditioned reaction liquid pH and temperature of reaction are that 8.5-9.5, temperature are 45 ℃-60 ℃ for the peak enzymolysis-ability reaction solution pH of the Alcalase of recommendation; Wherein said enzyme concentration is the 0.5%-4% that accounts for the fish scale collagen mass ratio; Wherein said enzyme-added before material solution cycling time be 5min; The wherein said reaction times is 10-60min; Wherein said " the speed change circulation of back low speed earlier at a high speed " promptly earlier reacts 20min under the recycle pump rotating speed of 150r/min, after the rotating speed of recycle pump is turned down to 100r/min reaction 6min, carry out speed change circulation enzymolysis-membrane sepn coupling reaction; Wherein adopting molecular weight cut-off in the ultra-filtration process is the Mierocrystalline cellulose flat sheet membrane of 3kDa-10kDa.
5. no-feed supplement enzymolysis according to claim 3-membrane sepn coupling prepares the method for fish scale collagen anti-oxidation peptide, it is characterized in that adopting molecular weight cut-off in the ultra-filtration process is the Mierocrystalline cellulose flat sheet membrane of 3kDa.
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102747125A (en) * | 2012-06-25 | 2012-10-24 | 宁波武盛化学有限公司 | Preparation method of antioxidative peptide of hairtail |
| CN103468772A (en) * | 2013-08-30 | 2013-12-25 | 国家海洋局第三海洋研究所 | Preparation process for fishery by-product source I type collagen antioxidation peptide |
| CN103540528A (en) * | 2013-10-17 | 2014-01-29 | 镇江五棵松生物科技有限公司 | Enzyme-membrane coupling reaction system with speed-changing circulation |
| CN103992386A (en) * | 2014-05-22 | 2014-08-20 | 浙江海洋学院 | Pseudosciaena crocea fish scale oxidation-resistant collagen peptide, and preparation method and application thereof |
| CN104762355A (en) * | 2015-03-04 | 2015-07-08 | 江苏大学 | Preparation method for fish scale collagen protein active peptide |
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| CN1635137A (en) * | 2003-12-29 | 2005-07-06 | 黑龙江省大豆技术开发研究中心 | Process for preparing soybean antioxidant peptides |
| CN1775950A (en) * | 2005-10-19 | 2006-05-24 | 由守谊 | Fishscale collagen production process |
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| CN1635137A (en) * | 2003-12-29 | 2005-07-06 | 黑龙江省大豆技术开发研究中心 | Process for preparing soybean antioxidant peptides |
| CN1775950A (en) * | 2005-10-19 | 2006-05-24 | 由守谊 | Fishscale collagen production process |
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102747125A (en) * | 2012-06-25 | 2012-10-24 | 宁波武盛化学有限公司 | Preparation method of antioxidative peptide of hairtail |
| CN103468772A (en) * | 2013-08-30 | 2013-12-25 | 国家海洋局第三海洋研究所 | Preparation process for fishery by-product source I type collagen antioxidation peptide |
| CN103540528A (en) * | 2013-10-17 | 2014-01-29 | 镇江五棵松生物科技有限公司 | Enzyme-membrane coupling reaction system with speed-changing circulation |
| CN103992386A (en) * | 2014-05-22 | 2014-08-20 | 浙江海洋学院 | Pseudosciaena crocea fish scale oxidation-resistant collagen peptide, and preparation method and application thereof |
| CN104762355A (en) * | 2015-03-04 | 2015-07-08 | 江苏大学 | Preparation method for fish scale collagen protein active peptide |
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