CN117265052A - Co-production preparation process of abalone antifreeze peptide and polysaccharide - Google Patents
Co-production preparation process of abalone antifreeze peptide and polysaccharide Download PDFInfo
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- CN117265052A CN117265052A CN202311194642.5A CN202311194642A CN117265052A CN 117265052 A CN117265052 A CN 117265052A CN 202311194642 A CN202311194642 A CN 202311194642A CN 117265052 A CN117265052 A CN 117265052A
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- 150000004676 glycans Chemical class 0.000 title claims abstract description 35
- 229920001282 polysaccharide Polymers 0.000 title claims abstract description 35
- 239000005017 polysaccharide Substances 0.000 title claims abstract description 35
- 108010053481 Antifreeze Proteins Proteins 0.000 title claims abstract description 23
- 238000002360 preparation method Methods 0.000 title claims abstract description 18
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 17
- 239000007788 liquid Substances 0.000 claims abstract description 36
- 102000004142 Trypsin Human genes 0.000 claims abstract description 28
- 108090000631 Trypsin Proteins 0.000 claims abstract description 28
- 239000012588 trypsin Substances 0.000 claims abstract description 28
- 239000012530 fluid Substances 0.000 claims abstract description 27
- 239000000706 filtrate Substances 0.000 claims abstract description 26
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 26
- 239000012528 membrane Substances 0.000 claims abstract description 17
- 210000001835 viscera Anatomy 0.000 claims abstract description 16
- 239000002994 raw material Substances 0.000 claims abstract description 14
- 102000004190 Enzymes Human genes 0.000 claims abstract description 13
- 108090000790 Enzymes Proteins 0.000 claims abstract description 13
- 238000000034 method Methods 0.000 claims abstract description 13
- 239000000203 mixture Substances 0.000 claims abstract description 10
- 239000006228 supernatant Substances 0.000 claims abstract description 9
- 230000000415 inactivating effect Effects 0.000 claims abstract description 8
- 238000001035 drying Methods 0.000 claims abstract description 7
- 239000002244 precipitate Substances 0.000 claims abstract description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 6
- 238000001556 precipitation Methods 0.000 claims abstract description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 12
- 239000007864 aqueous solution Substances 0.000 claims description 10
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 10
- 238000001914 filtration Methods 0.000 claims description 9
- 239000000919 ceramic Substances 0.000 claims description 6
- 238000001471 micro-filtration Methods 0.000 claims description 5
- 238000002390 rotary evaporation Methods 0.000 claims description 3
- 239000000243 solution Substances 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims 2
- 239000007921 spray Substances 0.000 claims 1
- 239000002699 waste material Substances 0.000 abstract description 5
- 238000012545 processing Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- MSWZFWKMSRAUBD-GASJEMHNSA-N 2-amino-2-deoxy-D-galactopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O MSWZFWKMSRAUBD-GASJEMHNSA-N 0.000 description 1
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 241000194020 Streptococcus thermophilus Species 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 229960002442 glucosamine Drugs 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000036449 good health Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000021049 nutrient content Nutrition 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000012465 retentate Substances 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
- C08B37/00—Preparation of polysaccharides not provided for in groups C08B1/00 - C08B35/00; Derivatives thereof
- C08B37/006—Heteroglycans, i.e. polysaccharides having more than one sugar residue in the main chain in either alternating or less regular sequence; Gellans; Succinoglycans; Arabinogalactans; Tragacanth or gum tragacanth or traganth from Astragalus; Gum Karaya from Sterculia urens; Gum Ghatti from Anogeissus latifolia; Derivatives thereof
- C08B37/0063—Glycosaminoglycans or mucopolysaccharides, e.g. keratan sulfate; Derivatives thereof, e.g. fucoidan
- C08B37/0066—Isolation or extraction of proteoglycans from organs
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Water Supply & Treatment (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Materials Engineering (AREA)
- Polymers & Plastics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to a abalone antifreeze peptide and polysaccharide co-production preparation process, which comprises the following steps: taking abalone viscera as a raw material, carrying out primary enzymolysis on the raw material by trypsin, and inactivating enzyme after the enzymolysis is finished to obtain primary enzymolysis liquid; centrifuging the primary enzymolysis liquid, and taking supernatant; performing primary ultrafiltration on the supernatant by using a 10000Da ultrafiltration membrane to obtain a first filtrate and a first trapped fluid; carrying out secondary enzymolysis on the first trapped fluid by adopting trypsin, and inactivating enzyme after the secondary enzymolysis is finished to obtain secondary enzymolysis fluid; performing secondary ultrafiltration on the secondary enzymolysis liquid by using 10000Da ultrafiltration membrane to obtain second filtrate and second trapped fluid; combining the first filtrate and the second filtrate to obtain a filtrate mixture, concentrating and drying the filtrate mixture to obtain the antifreeze peptide; and (3) placing the second trapped fluid in absolute ethyl alcohol for precipitation, collecting the precipitate and drying to obtain the polysaccharide. According to the invention, the abalone viscera is used as a raw material, and the antifreeze peptide and the polysaccharide are prepared by co-production in a set of process flows, so that the abalone viscera waste is utilized, and the comprehensive utilization of the abalone is improved.
Description
Technical Field
The invention relates to the technical field of deep processing of aquatic products, in particular to a co-production preparation process of abalone antifreeze peptide and polysaccharide.
Background
The abalone sea mollusk has rich in-vivo protein, sugar, fat and other nutrient contents, has high edible value and good health care effect, so that the abalone-related products are deeply favored by consumers, and the processing rate and processing level of the abalone are improved year by year. However, during processing, the viscera of abalone are often peeled away in order to avoid the appearance and taste being impaired. The viscera of abalone account for 20-30% of the total weight, and the viscera contain higher nutritional ingredients, if a large amount of viscera of abalone are abandoned, serious resource waste and environmental pollution can be caused. Therefore, research on the extraction technology of the nutrient components in the viscera of the abalone has important practical significance for improving the comprehensive utilization of the abalone and protecting the environment.
Disclosure of Invention
The invention aims to provide a co-production preparation process of abalone antifreeze peptide and polysaccharide, which takes abalone viscera as raw materials and uses a set of process flow to co-produce the antifreeze peptide and the polysaccharide, so that the abalone viscera waste is utilized, and the comprehensive utilization of abalone is improved.
In order to achieve the aim, the invention discloses a abalone antifreeze peptide and polysaccharide co-production preparation process, which comprises the following steps:
primary enzymolysis: taking abalone viscera as a raw material, carrying out primary enzymolysis on the raw material by trypsin, and inactivating enzyme after the enzymolysis is finished to obtain primary enzymolysis liquid;
and (3) filtering: centrifuging the primary enzymolysis liquid, and taking supernatant;
primary ultrafiltration: performing primary ultrafiltration on the supernatant by using a 10000Da ultrafiltration membrane to obtain a first filtrate and a first trapped fluid;
and (3) secondary enzymolysis: carrying out secondary enzymolysis on the first trapped fluid by adopting trypsin, and inactivating enzyme after the secondary enzymolysis is finished to obtain secondary enzymolysis fluid;
secondary ultrafiltration: performing secondary ultrafiltration on the secondary enzymolysis liquid by using 10000Da ultrafiltration membrane to obtain second filtrate and second trapped fluid;
preparation of antifreeze peptide: combining the first filtrate and the second filtrate to obtain a filtrate mixture, concentrating and drying the filtrate mixture to obtain the antifreeze peptide;
polysaccharide preparation: and (3) placing the second trapped fluid in absolute ethyl alcohol for precipitation, collecting the precipitate and drying to obtain the polysaccharide.
Preferably, in the primary enzymolysis step, the abalone viscera are homogenized and then subjected to primary enzymolysis by trypsin, wherein the addition amount of the trypsin is 10-13% of the weight of the raw materials; the trypsin participates in primary enzymolysis in an aqueous solution mode, and the solid-to-liquid ratio of the aqueous solution of the trypsin is 1:18-24; the pH value is 7.8-8.2 during primary enzymolysis, the time is 2-3 h, and the enzyme is inactivated for 20-40 min at 70-90 ℃ after the primary enzymolysis is finished.
Preferably, the method further comprises a decolorizing step performed after the primary ultrafiltration step and before the filtration step, which is: adding 60-100 meshes of activated carbon into the primary enzymolysis liquid, uniformly stirring, standing for 3-4 hours, wherein the addition amount of the activated carbon is 1-3% of the weight of the enzymolysis liquid in sequence.
Preferably, in the filtering step, the primary enzymolysis liquid is centrifuged by a continuous centrifuge, and the centrifugal speed is 8000-10000 rpm.
Preferably, in the filtration step, the supernatant is also subjected to microfiltration through a 200 μm ceramic membrane.
Preferably, in the secondary enzymolysis step, the adding amount of trypsin is 5-6% of the weight of the first trapped fluid, the trypsin participates in the secondary enzymolysis in an aqueous solution mode, and the solid-to-liquid ratio of the aqueous solution of the trypsin is 1:18-24; the pH value is 7.8-8.2 during the secondary enzymolysis, the time is 2-3 h, and the enzyme is inactivated for 20-40 min at 70-90 ℃ after the secondary enzymolysis is finished.
Preferably, the secondary enzymolysis liquid is subjected to microfiltration through a 200um ceramic membrane and then secondary ultrafiltration.
Preferably, in the antifreeze peptide preparation step, the filtrate mixture is concentrated by vacuum rotary evaporation at 55-60 ℃ and then spray-dried to obtain the antifreeze peptide.
Preferably, in the polysaccharide preparation step, the second trapped fluid is placed in absolute ethyl alcohol with the volume of 3-5 times of that of the second trapped fluid to be precipitated for 2-5 hours, and the precipitate is collected and dried at the temperature of 40-50 ℃ to obtain the polysaccharide.
The invention has the following beneficial effects:
according to the invention, the antifreeze peptide and the polysaccharide can be prepared in a co-production way through a set of process flow, the preparation efficiency is higher, the adopted raw materials are waste abalone viscera, the waste is utilized, the comprehensive utilization of abalone is improved, and the environment is protected.
Detailed Description
The present invention will be described in further detail with reference to the following examples in order to make the objects, technical solutions and advantages of the present invention more apparent.
The invention discloses a abalone antifreeze peptide and polysaccharide co-production preparation process, which comprises the following steps:
primary enzymolysis: the abalone viscera is taken as a raw material, homogenized and treated, the raw material is subjected to primary enzymolysis by adopting trypsin, the adding amount of the trypsin is 10.75% of the weight of the raw material, the trypsin participates in the primary enzymolysis in an aqueous solution mode, and the solid-liquid ratio of the aqueous solution of the trypsin is 1:20. The pH value is regulated to 8.0 during primary enzymolysis, and the time is 2.75 hours. After the enzymolysis is finished, inactivating enzyme for 30min at 85 ℃ to obtain primary enzymolysis liquid. The protein content in the primary enzymolysis liquid is about 36.37% and the polysaccharide content is about 16.5% by measurement.
Decoloring: adding 80-mesh active carbon into the primary enzymolysis liquid, stirring uniformly, and standing for 3h. The addition amount of the activated carbon is 1% of the weight of the primary enzymolysis liquid.
And (3) filtering: and (3) centrifuging the primary enzymolysis liquid by a continuous centrifuge, wherein the centrifuging speed is 8000rpm. After centrifugal treatment, the active carbon can be removed, and the supernatant is taken and subjected to microfiltration treatment by a 200um ceramic membrane to obtain clarified primary enzymolysis liquid.
Primary ultrafiltration: and performing primary ultrafiltration on the clarified primary enzymolysis liquid by using a 10000Da ultrafiltration membrane to obtain a first filtrate and a first trapped fluid. The molecular weight of polysaccharide in the primary enzymolysis liquid is mostly more than 10 kDa, and 82.11 percent of polysaccharide in the primary enzymolysis liquid is intercepted by a membrane with the interception molecular weight of 10 kDa. While 54.71% of the water-soluble protein in the primary enzymolysis liquid is trapped by a membrane with the molecular weight of 10 kDa, which indicates that the other part of macromolecular protein is hydrolyzed into micromolecular polypeptide by enzyme and penetrates the membrane with the molecular weight of 10 kDa.
And (3) secondary enzymolysis: and carrying out secondary enzymolysis on the first trapped fluid by adopting trypsin, wherein the adding amount of the trypsin is 5% of the weight of the first trapped fluid, and the trypsin participates in the secondary enzymolysis in an aqueous solution mode, and the solid-to-liquid ratio of the aqueous solution of the trypsin is 1:20. And during secondary enzymolysis, the pH value is regulated to 8.0, and the time is 2.75 hours. And after the secondary enzymolysis is finished, inactivating enzyme for 30min at 85 ℃ to obtain secondary enzymolysis liquid.
Secondary ultrafiltration: and (3) carrying out microfiltration on the secondary enzymolysis liquid by using a 200um ceramic membrane, and then carrying out secondary ultrafiltration on the secondary enzymolysis liquid by using a 10000Da ultrafiltration membrane to obtain a second filtrate and a second trapped fluid. The second retentate was lyophilized and its polysaccharide and protein content was determined to be the highest, 51.75%.
Preparation of antifreeze peptide: and combining the first filtrate and the second filtrate to obtain a filtrate mixture, concentrating the filtrate mixture by vacuum rotary evaporation at the temperature of 60 ℃, and then performing spray drying to obtain the antifreeze peptide.
Polysaccharide preparation: and (3) placing the second trapped fluid in absolute ethyl alcohol with the volume being 3-5 times of that of the second trapped fluid to precipitate for 2-5 hours, collecting the precipitate and drying the precipitate at the temperature of 40-50 ℃ to obtain the polysaccharide.
Through inspection, the yield of the antifreeze peptide product is 4.4%, and the molecular weight is less than 1000Da and the ratio is 98%. The freeze-proof activity experiment shows that the polypeptide streptococcus thermophilus has freeze survival rate up to 38.93% and excellent freeze-proof activity. The polysaccharide content is 51.75%, and is mainly composed of mannose, glucosamine, galactosamine, galactose, glucose, xylose, fucose, etc.
The present invention is not limited to the above-mentioned embodiments, and any changes or substitutions that can be easily understood by those skilled in the art within the technical scope of the present invention are intended to be included in the scope of the present invention.
Claims (9)
1. A process for co-producing abalone antifreeze peptide and polysaccharide is characterized by comprising the following steps:
primary enzymolysis: taking abalone viscera as a raw material, carrying out primary enzymolysis on the raw material by trypsin, and inactivating enzyme after the enzymolysis is finished to obtain primary enzymolysis liquid;
and (3) filtering: centrifuging the primary enzymolysis liquid, and taking supernatant;
primary ultrafiltration: performing primary ultrafiltration on the supernatant by using a 10000Da ultrafiltration membrane to obtain a first filtrate and a first trapped fluid;
and (3) secondary enzymolysis: carrying out secondary enzymolysis on the first trapped fluid by adopting trypsin, and inactivating enzyme after the secondary enzymolysis is finished to obtain secondary enzymolysis fluid;
secondary ultrafiltration: performing secondary ultrafiltration on the secondary enzymolysis liquid by using 10000Da ultrafiltration membrane to obtain second filtrate and second trapped fluid;
preparation of antifreeze peptide: combining the first filtrate and the second filtrate to obtain a filtrate mixture, concentrating and drying the filtrate mixture to obtain the antifreeze peptide;
polysaccharide preparation: and (3) placing the second trapped fluid in absolute ethyl alcohol for precipitation, collecting the precipitate and drying to obtain the polysaccharide.
2. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the primary enzymolysis step, the abalone viscera are homogenized and then subjected to primary enzymolysis by trypsin, wherein the addition amount of the trypsin is 10-13% of the weight of the raw materials; the trypsin participates in primary enzymolysis in an aqueous solution mode, and the solid-to-liquid ratio of the aqueous solution of the trypsin is 1:18-24; the pH value is 7.8-8.2 during primary enzymolysis, the time is 2-3 h, and the enzyme is inactivated for 20-40 min at 70-90 ℃ after the primary enzymolysis is finished.
3. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: further comprising a decolorizing step performed after the primary ultrafiltration step and before the filtration step, which is: adding 60-100 meshes of activated carbon into the primary enzymolysis liquid, uniformly stirring, standing for 3-4 hours, wherein the addition amount of the activated carbon is 1-3% of the weight of the enzymolysis liquid in sequence.
4. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the filtering step, the primary enzymolysis liquid is centrifuged by a continuous centrifuge, and the centrifugal speed is 8000-10000 rpm.
5. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the filtering step, the supernatant is also subjected to microfiltration by a 200um ceramic membrane.
6. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the secondary enzymolysis step, the adding amount of trypsin is 5-6% of the weight of the first trapped fluid, the trypsin participates in the secondary enzymolysis in a water solution mode, and the solid-liquid ratio of the water solution of the trypsin is 1:18-24; the pH value is 7.8-8.2 during the secondary enzymolysis, the time is 2-3 h, and the enzyme is inactivated for 20-40 min at 70-90 ℃ after the secondary enzymolysis is finished.
7. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: the secondary enzymolysis liquid is filtered by a 200um ceramic membrane and then is subjected to secondary ultrafiltration.
8. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the preparation step of the antifreeze peptide, the filtrate mixture is concentrated by vacuum rotary evaporation at 55-60 ℃ and then is spray dried to obtain the antifreeze peptide.
9. The process for the co-production of Bao Kangdong peptide and polysaccharide according to claim 1, wherein: in the polysaccharide preparation step, the second trapped fluid is placed in absolute ethyl alcohol with the volume of 3-5 times of that of the second trapped fluid to be precipitated for 2-5 hours, and the precipitate is collected and dried at the temperature of 40-50 ℃ to obtain the polysaccharide.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202311194642.5A CN117265052A (en) | 2023-09-15 | 2023-09-15 | Co-production preparation process of abalone antifreeze peptide and polysaccharide |
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| Application Number | Priority Date | Filing Date | Title |
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| CN202311194642.5A CN117265052A (en) | 2023-09-15 | 2023-09-15 | Co-production preparation process of abalone antifreeze peptide and polysaccharide |
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| CN117265052A true CN117265052A (en) | 2023-12-22 |
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| CN202311194642.5A Pending CN117265052A (en) | 2023-09-15 | 2023-09-15 | Co-production preparation process of abalone antifreeze peptide and polysaccharide |
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- 2023-09-15 CN CN202311194642.5A patent/CN117265052A/en active Pending
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