CN105112478B - Preparation method of squid skin active polypeptide - Google Patents
Preparation method of squid skin active polypeptide Download PDFInfo
- Publication number
- CN105112478B CN105112478B CN201510242409.9A CN201510242409A CN105112478B CN 105112478 B CN105112478 B CN 105112478B CN 201510242409 A CN201510242409 A CN 201510242409A CN 105112478 B CN105112478 B CN 105112478B
- Authority
- CN
- China
- Prior art keywords
- squid skin
- enzymolysis liquid
- active polypeptide
- enzymolysis
- squid
- 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.)
- Active
Links
- 241000238366 Cephalopoda Species 0.000 title claims abstract description 70
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 28
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 25
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 25
- 238000002360 preparation method Methods 0.000 title claims abstract description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims abstract description 45
- 239000007788 liquid Substances 0.000 claims abstract description 43
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 claims abstract description 37
- 102000004190 Enzymes Human genes 0.000 claims abstract description 33
- 108090000790 Enzymes Proteins 0.000 claims abstract description 33
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 claims abstract description 22
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 21
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims abstract description 18
- 238000000034 method Methods 0.000 claims abstract description 17
- 238000005406 washing Methods 0.000 claims abstract description 15
- 238000003756 stirring Methods 0.000 claims abstract description 13
- 235000017557 sodium bicarbonate Nutrition 0.000 claims abstract description 11
- 229910000030 sodium bicarbonate Inorganic materials 0.000 claims abstract description 11
- 238000002791 soaking Methods 0.000 claims abstract description 10
- 230000007935 neutral effect Effects 0.000 claims abstract description 9
- 229910052757 nitrogen Inorganic materials 0.000 claims abstract description 9
- 238000010438 heat treatment Methods 0.000 claims abstract description 7
- 238000004140 cleaning Methods 0.000 claims abstract description 6
- 238000001816 cooling Methods 0.000 claims abstract description 6
- 230000000415 inactivating effect Effects 0.000 claims abstract description 6
- 238000005360 mashing Methods 0.000 claims abstract description 6
- 239000006228 supernatant Substances 0.000 claims abstract description 6
- 230000008569 process Effects 0.000 claims description 8
- 108090000145 Bacillolysin Proteins 0.000 claims description 6
- 108091005658 Basic proteases Proteins 0.000 claims description 6
- 108091005507 Neutral proteases Proteins 0.000 claims description 6
- 102000035092 Neutral proteases Human genes 0.000 claims description 6
- 102000004142 Trypsin Human genes 0.000 claims description 6
- 108090000631 Trypsin Proteins 0.000 claims description 6
- 239000012588 trypsin Substances 0.000 claims description 6
- 230000007062 hydrolysis Effects 0.000 abstract description 8
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 8
- 238000006243 chemical reaction Methods 0.000 abstract description 6
- 238000004519 manufacturing process Methods 0.000 abstract description 5
- 239000000243 solution Substances 0.000 description 25
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 230000003078 antioxidant effect Effects 0.000 description 5
- 102000008186 Collagen Human genes 0.000 description 3
- 108010035532 Collagen Proteins 0.000 description 3
- 238000007664 blowing Methods 0.000 description 3
- 229920001436 collagen Polymers 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 238000009776 industrial production Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- -1 DPPH free radical Chemical class 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000017525 heat dissipation Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 210000001835 viscera Anatomy 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
The invention discloses a preparation method of squid skin active polypeptide, which comprises the following steps: (1) cleaning and mashing squid skin, adding a sodium hydroxide solution, soaking for 24-30 h, washing with water until the pH value is neutral, adding an n-butyl alcohol solution, stirring for 16-24 h, washing with water, and draining; (2) adding water which is 90-95 times of the weight of the squid skin into the drained squid skin, uniformly stirring, heating to 40-60 ℃, preserving heat for 3-5 hours, and adjusting the pH value to 8-9 to obtain a primary enzymolysis liquid; (3) adding a complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 20-30 min at 40-50 ℃, inactivating enzymes, and cooling to obtain a final enzymolysis liquid, wherein nitrogen is continuously blown into the chelating liquid during the enzymolysis; (4) and centrifuging the final enzymolysis liquid, and collecting supernatant to obtain the squid skin active polypeptide solution. The method has the advantages of simple process steps, easily controlled reaction process, strong operability, short production period and high squid skin hydrolysis degree.
Description
Technical Field
The invention relates to the technical field of aquatic product deep processing, in particular to a preparation method of squid skin active polypeptide.
Background
In recent years, with the rapid development of the oceanic squid fishing industry in China, squids increasingly become the main marine economic mollusks and aquatic product processing raw materials in China. At present, the processing and utilization technology content of the squid in China is low, and about 35% of squid heads, feet, skin, viscera and other byproducts are generated in the production, wherein the squid skin accounts for about 8% -13%.
The squid skin has a high collagen content, which is about 80% of the dry weight. The absorption rate of collagen polypeptide is nearly 100%, and the collagen polypeptide has the functions of resisting ulcer, reducing blood pressure and promoting Ca2+Absorption and the like. Therefore, the polypeptide substance with antioxidant activity is obtained from the squid skin, which is beneficial to greatly improving the added value of the squid skin.
Chinese patent application publication No. CN 102217699A, application publication No. 2011.10.19 discloses a preparation method of squid skin protein active peptide, which comprises the steps of cleaning squid skin, cutting into blocks, adding NaOH aqueous solution, soaking for 2-8 days for decolorization, and washing to neutral pH; addition of Ca (OH)2Soaking the mixture in the solution for 2-4 days for color fixation, and washing the mixture with water until the pH value is neutral; treating the fish skin in neutral water with the pH value of 55-75 ℃ for 0.5-1.5 h, filtering, removing insoluble protein, and extracting to obtain fish skin protein liquid; and finally, carrying out high-pressure treatment on the liquid at 110-121 ℃ for 30-120 min to obtain the squid skin protein active peptide. The preparation method has the following disadvantages: (1) the production period of the whole preparation method is long; (2) the preparation of the bioactive peptide by treating the squid skin protein with high-pressure hot water needs to be carried out under high-pressure conditions, the process conditions are strict, the operability is poor, and the squid skin waterInsufficient hydrolysis, low degree of hydrolysis and low antioxidant activity.
Disclosure of Invention
The invention aims to solve the problems in the prior art and provides the preparation method of the squid skin active polypeptide, which has the advantages of simple process steps, easily controlled reaction process, strong operability, short production period and high squid skin hydrolysis degree.
In order to achieve the purpose, the invention adopts the following technical scheme:
a preparation method of squid skin active polypeptide comprises the following steps:
(1) washing and mashing squid skin, adding a sodium hydroxide solution, soaking for 24-30 h, washing with water until the pH value is neutral, adding an n-butyl alcohol solution, stirring for 16-24 h, washing with water, and draining. Soaking in sodium hydroxide to remove foreign proteins; soaking in n-butanol solution to remove lipid.
(2) Adding water which is 90-95 times of the weight of the drained squid skin into the drained squid skin, uniformly stirring, heating to 40-60 ℃, preserving heat for 3-5 hours, and adjusting the pH value to 8-9 to obtain a primary enzymolysis liquid. Heating squid skin under 40~60 ℃, utilizing the enzyme of squid skin self to carry out preliminary enzymolysis, not only be favorable to improving the degree of hydrolysis, can reduce the use amount of compound enzyme in the follow-up enzymolysis process moreover, be favorable to reduce cost.
(3) Adding complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 20-30 min at 40-50 ℃, inactivating enzyme, and cooling to obtain final enzymolysis liquid, wherein nitrogen is continuously blown into the chelating liquid during the enzymolysis. The invention carries out enzymolysis under the ultrasonic condition to improve the enzymolysis efficiency and effect, but the ultrasonic wave has heat effect at the same time, and can change the temperature of the whole system, so that the whole enzymolysis process is unstable, therefore, the invention solves the problems by introducing nitrogen during enzymolysis, and the introduced nitrogen can play a role of stirring, so that the raw materials of the enzymolysis reaction can be mixed more uniformly, and the enzymolysis is more sufficient; secondly, the heat dissipation function is achieved, so that heat generated by enzymolysis reaction and ultrasonic waves can be dissipated in time, and the temperature is kept stable during enzymolysis; the introduction amount of nitrogen is based on that the primary enzymolysis liquid does not splash; NaHCO 23The solution plays a role of buffering,so as to stabilize the pH value of the whole reaction system.
(4) And centrifuging the final enzymolysis liquid, and collecting supernatant to obtain the squid skin active polypeptide solution.
Preferably, in the step (1), 30-50 ml of sodium hydroxide solution is added to each gram of squid skin, and the mass percentage concentration of the sodium hydroxide solution is 0.2-0.5%.
Preferably, in the step (1), 30-50 ml of n-butyl alcohol solution is added to each gram of squid skin, and the mass percentage concentration of the n-butyl alcohol solution is 10-15%.
Preferably, in the step (3), 14000-15000 u of complex enzyme is added into each gram of the primary enzymolysis liquid, and the complex enzyme comprises the following enzymes in percentage by mass: 20-30% of alkaline protease, 10-20% of trypsin and the balance of neutral protease. According to the invention, the enzyme is screened, and the squid skin is subjected to enzymolysis by selecting the compound enzyme consisting of the alkaline protease, the trypsin and the neutral protease, so that the enzymolysis efficiency is high, the enzymolysis effect is good, and the antioxidant activity of the obtained polypeptide is high.
Preferably, in the step (3), the addition amount of the sodium bicarbonate is 0.5-1% of the mass of the primary enzymolysis liquid.
Preferably, in the step (3), the ultrasonic process conditions are as follows: the ultrasonic frequency is 25-40 kHz, and the power is 100-120W.
Therefore, the beneficial effects of the invention are as follows: the method has the advantages that the compound enzyme is used as the suitable enzyme for preparing the polypeptide from the squid skin, the preparation process of the squid skin active polypeptide is optimized, the process steps are simple, the reaction process is easy to control, the operability is strong, the production period is short, the hydrolysis degree of the squid skin is high, the obtained squid skin active polypeptide has high antioxidant activity, and the theoretical basis is provided for industrial production.
Detailed Description
The invention is further described below by means of specific embodiments.
In the present invention, all percentages are by weight unless otherwise specified, all equipment and materials are commercially available or commonly used in the industry, and the methods in the following examples are conventional in the art unless otherwise specified.
Example 1
(1) Cleaning squid skin, mashing, adding a sodium hydroxide solution with the mass percentage concentration of 0.2%, adding 30ml of the sodium hydroxide solution into each gram of the squid skin, soaking for 24 hours, washing with water until the pH value is neutral, adding a n-butyl alcohol solution with the mass percentage concentration of 10%, adding 30ml of the n-butyl alcohol solution into each gram of the squid skin, stirring for 16 hours, washing with water, and draining.
(2) Adding water which is 90 times of the weight of the squid skin into the drained squid skin, uniformly stirring, heating to 40 ℃, keeping the temperature for 3 hours, and adjusting the pH value to 8 to obtain a primary enzymolysis liquid.
(3) Adding complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 20min at 40 ℃, inactivating enzyme, and cooling to obtain final enzymolysis liquid, continuously blowing nitrogen into chelating liquid during enzymolysis, adding 14000u of complex enzyme into each gram of primary enzymolysis liquid, wherein the complex enzyme comprises the following enzymes in percentage by mass: 20% of alkaline protease, 10% of trypsin and the balance of neutral protease; the adding amount of the sodium bicarbonate is 0.5 percent of the mass of the primary enzymolysis liquid; the ultrasonic process conditions are as follows: the ultrasonic frequency is 25kHz, and the power is 100W.
(4) And centrifuging the final enzymolysis liquid, and collecting supernatant to obtain the squid skin active polypeptide solution.
Example 2
(1) Cleaning squid skin, mashing, adding a sodium hydroxide solution with the mass percentage concentration of 0.5%, adding 50ml of the sodium hydroxide solution into each gram of the squid skin, soaking for 30h, washing with water until the pH value is neutral, adding a n-butyl alcohol solution with the mass percentage concentration of 15%, adding 50ml of the n-butyl alcohol solution into each gram of the squid skin, stirring for 24h, washing with water, and draining.
(2) Adding water with the mass 95 times of that of the drained squid skin into the drained squid skin, uniformly stirring, heating to 60 ℃, keeping the temperature for 5 hours, and adjusting the pH to 9 to obtain a primary enzymolysis liquid.
(3) Adding complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 30min at 50 ℃, inactivating enzyme, and cooling to obtain final enzymolysis liquid, continuously blowing nitrogen into chelating liquid during enzymolysis, adding 15000u of complex enzyme into each gram of primary enzymolysis liquid, wherein the complex enzyme comprises the following enzymes in percentage by mass: 30% of alkaline protease, 20% of trypsin and the balance of neutral protease; the adding amount of the sodium bicarbonate is 1 percent of the mass of the primary enzymolysis liquid; the ultrasonic process conditions are as follows: the ultrasonic frequency is 40kHz and the power is 120W.
(4) And centrifuging the final enzymolysis liquid, and collecting supernatant to obtain the squid skin active polypeptide solution.
Example 3
(1) Cleaning squid skin, mashing, adding a sodium hydroxide solution with the mass percentage concentration of 0.3%, adding 40 ml of the sodium hydroxide solution into each gram of the squid skin, soaking for 25 h, washing with water until the pH value is neutral, adding a n-butanol solution with the mass percentage concentration of 12%, adding 40 ml of the n-butanol solution into each gram of the squid skin, stirring for 20h, washing with water, and draining.
(2) Adding water which is 92 times of the weight of the squid skin into the drained squid skin, uniformly stirring, heating to 45 ℃, keeping the temperature for 4 hours, and adjusting the pH value to 8.5 to obtain a primary enzymolysis liquid.
(3) Adding complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 25min at 45 ℃, inactivating enzyme, and cooling to obtain final enzymolysis liquid, continuously blowing nitrogen into the chelating liquid during the enzymolysis, adding 14500u of complex enzyme into each gram of the primary enzymolysis liquid, wherein the complex enzyme comprises the following enzymes in percentage by mass: 25% of alkaline protease, 12% of trypsin and the balance of neutral protease; the adding amount of the sodium bicarbonate is 0.6 percent of the mass of the primary enzymolysis liquid; the ultrasonic process conditions are as follows: the ultrasonic frequency is 30kHz and the power is 110W.
(4) And centrifuging the final enzymolysis liquid, and collecting supernatant to obtain the squid skin active polypeptide solution.
The hydrolysis degree of the squid skin is more than 18.5%, and the DPPH free radical clearance rate of the obtained squid skin active polypeptide is more than 45%. Therefore, the preparation method disclosed by the invention has the advantages that the squid skin hydrolysis degree is high, the obtained squid skin active polypeptide has high antioxidant activity, and a theoretical basis is provided for industrial production.
The above-described embodiments are only preferred embodiments of the present invention, and are not intended to limit the present invention in any way, and other variations and modifications may be made without departing from the spirit of the invention as set forth in the claims.
Claims (4)
1. A preparation method of squid skin active polypeptide is characterized by comprising the following steps:
(1) cleaning and mashing squid skin, adding a sodium hydroxide solution, soaking for 24-30 h, washing with water until the pH value is neutral, adding an n-butyl alcohol solution, stirring for 16-24 h, washing with water, and draining;
(2) adding water which is 90-95 times of the weight of the squid skin into the drained squid skin, uniformly stirring, heating to 40-60 ℃, preserving heat for 3-5 hours, and adjusting the pH value to 8-9 to obtain a primary enzymolysis liquid;
(3) adding a complex enzyme and sodium bicarbonate into the primary enzymolysis liquid, performing ultrasonic enzymolysis for 20-30 min at 40-50 ℃, inactivating enzymes, and cooling to obtain a final enzymolysis liquid, wherein nitrogen is continuously blown into the chelating liquid during the enzymolysis;
(4) centrifuging the final enzymolysis liquid, and collecting supernatant to obtain squid skin active polypeptide solution;
in the step (3), 14000-15000 u of complex enzyme is added into each gram of the primary enzymolysis liquid, and the complex enzyme comprises the following enzymes in percentage by mass: 20-30% of alkaline protease, 10-20% of trypsin and the balance of neutral protease;
in the step (3), the addition amount of the sodium bicarbonate is 0.5-1% of the mass of the primary enzymolysis liquid.
2. The method for preparing squid skin active polypeptide according to claim 1, wherein 30-50 ml of sodium hydroxide solution is added to each gram of squid skin in the step (1), and the mass percentage concentration of the sodium hydroxide solution is 0.2-0.5%.
3. The method for preparing squid skin active polypeptide according to claim 1, wherein 30-50 ml of n-butanol solution is added to each gram of squid skin in the step (1), and the mass percentage concentration of the n-butanol solution is 10-15%.
4. The method for preparing squid skin active polypeptide according to claim 1, wherein in the step (3), the ultrasonic process conditions are as follows: the ultrasonic frequency is 25-40 kHz, and the power is 100-120W.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510242409.9A CN105112478B (en) | 2015-05-14 | 2015-05-14 | Preparation method of squid skin active polypeptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510242409.9A CN105112478B (en) | 2015-05-14 | 2015-05-14 | Preparation method of squid skin active polypeptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN105112478A CN105112478A (en) | 2015-12-02 |
| CN105112478B true CN105112478B (en) | 2021-05-18 |
Family
ID=54660584
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510242409.9A Active CN105112478B (en) | 2015-05-14 | 2015-05-14 | Preparation method of squid skin active polypeptide |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN105112478B (en) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106632668B (en) * | 2017-01-13 | 2020-04-14 | 上海华惠海洋生物科技有限公司 | Squid collagen polypeptide and preparation method and application of iron complex thereof |
| CN106946977A (en) * | 2017-02-13 | 2017-07-14 | 浙江海洋大学 | A kind of extracting method of squid active peptides |
| CN107853696A (en) * | 2017-11-21 | 2018-03-30 | 荣成海锐芯生物科技有限公司 | A kind of method that polypeptide oral liquor is prepared using blue and white fish enzymolysis |
| CN107912768B (en) * | 2017-12-22 | 2020-12-11 | 东阿阿胶股份有限公司 | Donkey placenta extract and preparation method thereof |
| CN108517343B (en) * | 2018-04-26 | 2021-02-02 | 厦门元之道生物科技有限公司 | Preparation method of porphyra yezoensis antioxidant protein peptide |
| CN110564800B (en) * | 2019-09-25 | 2023-06-06 | 浙江海洋大学 | Preparation method of squid skin protein Maillard peptide liquid with antioxidant activity |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101003827A (en) * | 2007-01-09 | 2007-07-25 | 中国海洋大学 | Method for preparing bioactive peptide of collagen from squid skin, and application |
| CN102676620A (en) * | 2011-12-20 | 2012-09-19 | 浙江省海洋开发研究院 | Preparation method of high-molecular-weight squid skin collagen |
| CN102690853A (en) * | 2012-03-22 | 2012-09-26 | 浙江省海洋开发研究院 | Preparation method of sleeve-fish skin low-molecular-weight collagen peptide |
-
2015
- 2015-05-14 CN CN201510242409.9A patent/CN105112478B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101003827A (en) * | 2007-01-09 | 2007-07-25 | 中国海洋大学 | Method for preparing bioactive peptide of collagen from squid skin, and application |
| CN102676620A (en) * | 2011-12-20 | 2012-09-19 | 浙江省海洋开发研究院 | Preparation method of high-molecular-weight squid skin collagen |
| CN102690853A (en) * | 2012-03-22 | 2012-09-26 | 浙江省海洋开发研究院 | Preparation method of sleeve-fish skin low-molecular-weight collagen peptide |
Non-Patent Citations (2)
| Title |
|---|
| 室温下超声辅助合成乙酸正丁酯的研究;陈曦等;《2009年功率超声论文集》;20091231;第82页最后1段 * |
| 超声催化水解法制邻氯苯甲醛的影响因素;许晓东等;《化学工程》;20041031;第32卷(第5期);第69页摘要，第71-72页第2.5节 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN105112478A (en) | 2015-12-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN105112478B (en) | Preparation method of squid skin active polypeptide | |
| CN112062834B (en) | Deep sea fish skin collagen peptide and extraction and preparation method thereof | |
| CN100489016C (en) | Method of extracting collagen and method of using collagen to prepare collagen protein | |
| WO2021142880A1 (en) | Method for producing clam active peptide | |
| CN109897101B (en) | Collagen tripeptide and production method and application thereof | |
| CN111944866B (en) | Method for preparing small molecular collagen peptide of yak leather by continuous rotary steaming desolventizing double enzymolysis | |
| CN111363772A (en) | Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof | |
| CN103392900A (en) | Method for preparing shrimp protein powder through shrimp hydrolysis | |
| CN112608968B (en) | Method for producing fish collagen peptide by using tilapia mossambica scale as raw material | |
| CN102732592A (en) | Method for preparing freshwater fish bone gelatin by enzyme process | |
| CN110117632B (en) | Method for improving antioxidant stability of watermelon seed polypeptide by combining ultrasonic and double enzymolysis | |
| CN111493205A (en) | Fish protein hydrolysate and preparation method thereof | |
| CN112724245A (en) | Method for extracting micromolecular collagen peptide by fish scale enzymolysis | |
| CN109355336B (en) | Method for extracting cow hide collagen | |
| CN114634961B (en) | Preparation method of oyster oligopeptide powder with multiple bioactivity functions | |
| CN104131060B (en) | Corbicula fluminea anti-oxidative peptide and preparation method thereof | |
| CN110229859A (en) | A kind of efficient preparation process of the anti-oxidant calcium ion chelating peptide in Optimization of Low Value Fish visceral protein source | |
| CN106591407A (en) | Fish collagen powder and preparing method thereof | |
| CN110679858A (en) | Method for extracting calcium nutrient from ox bone | |
| CN103667227B (en) | A kind of fractional precipitation extracts chymotrypsinogen and the method for trypsinogen | |
| CN107488696B (en) | Chicken bone double-enzymolysis method | |
| CN108396054A (en) | A method of enzymolysis Antarctic Ice fish prepares oligopeptide | |
| CN110643660B (en) | Method for preparing antioxidant peptide by donkey hide protease hydrolysis under assistance of ultrasound | |
| CN109295140A (en) | A kind of preparation method of Japanese croaker air bladder collagen protein source dipeptidyl peptidase-IV peptide for inhibiting | |
| CN108277247A (en) | The method that antioxidant activity polypeptide is extracted from squid spawn tangled gland |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |