CN111484893A - Method for synchronously preparing fish roe essential oil and fish roe functional peptide - Google Patents
Method for synchronously preparing fish roe essential oil and fish roe functional peptide Download PDFInfo
- Publication number
- CN111484893A CN111484893A CN202010336233.4A CN202010336233A CN111484893A CN 111484893 A CN111484893 A CN 111484893A CN 202010336233 A CN202010336233 A CN 202010336233A CN 111484893 A CN111484893 A CN 111484893A
- Authority
- CN
- China
- Prior art keywords
- fish roe
- roe
- fish
- functional peptide
- essential oil
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 241000251468 Actinopterygii Species 0.000 title claims abstract description 71
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 49
- 238000000034 method Methods 0.000 title claims abstract description 21
- 239000000341 volatile oil Substances 0.000 title claims abstract description 21
- 238000000605 extraction Methods 0.000 claims abstract description 20
- 239000006228 supernatant Substances 0.000 claims abstract description 12
- 102000029816 Collagenase Human genes 0.000 claims abstract description 10
- 108060005980 Collagenase Proteins 0.000 claims abstract description 10
- 102000004142 Trypsin Human genes 0.000 claims abstract description 10
- 108090000631 Trypsin Proteins 0.000 claims abstract description 10
- 229960002424 collagenase Drugs 0.000 claims abstract description 10
- 239000012588 trypsin Substances 0.000 claims abstract description 10
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 6
- 239000012530 fluid Substances 0.000 claims abstract description 6
- 239000007788 liquid Substances 0.000 claims abstract description 6
- 239000000843 powder Substances 0.000 claims abstract description 6
- 238000005374 membrane filtration Methods 0.000 claims abstract description 5
- 239000000706 filtrate Substances 0.000 claims abstract description 3
- 239000012528 membrane Substances 0.000 claims description 9
- 239000001273 butane Substances 0.000 claims description 8
- IJDNQMDRQITEOD-UHFFFAOYSA-N n-butane Chemical group CCCC IJDNQMDRQITEOD-UHFFFAOYSA-N 0.000 claims description 8
- OFBQJSOFQDEBGM-UHFFFAOYSA-N n-pentane Natural products CCCCC OFBQJSOFQDEBGM-UHFFFAOYSA-N 0.000 claims description 8
- 238000000926 separation method Methods 0.000 claims description 4
- 235000013305 food Nutrition 0.000 claims description 3
- 238000005119 centrifugation Methods 0.000 claims description 2
- 239000000047 product Substances 0.000 abstract description 4
- 230000009286 beneficial effect Effects 0.000 abstract description 2
- 230000001360 synchronised effect Effects 0.000 abstract description 2
- 241000700159 Rattus Species 0.000 description 13
- 239000004744 fabric Substances 0.000 description 10
- 230000000694 effects Effects 0.000 description 9
- 102000004196 processed proteins & peptides Human genes 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 150000001413 amino acids Chemical class 0.000 description 6
- 235000020776 essential amino acid Nutrition 0.000 description 6
- 239000003797 essential amino acid Substances 0.000 description 6
- 229930000680 A04AD01 - Scopolamine Natural products 0.000 description 5
- STECJAGHUSJQJN-GAUPFVANSA-N Hyoscine Natural products C1([C@H](CO)C(=O)OC2C[C@@H]3N([C@H](C2)[C@@H]2[C@H]3O2)C)=CC=CC=C1 STECJAGHUSJQJN-GAUPFVANSA-N 0.000 description 5
- STECJAGHUSJQJN-UHFFFAOYSA-N N-Methyl-scopolamin Natural products C1C(C2C3O2)N(C)C3CC1OC(=O)C(CO)C1=CC=CC=C1 STECJAGHUSJQJN-UHFFFAOYSA-N 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- STECJAGHUSJQJN-FWXGHANASA-N scopolamine Chemical compound C1([C@@H](CO)C(=O)O[C@H]2C[C@@H]3N([C@H](C2)[C@@H]2[C@H]3O2)C)=CC=CC=C1 STECJAGHUSJQJN-FWXGHANASA-N 0.000 description 5
- 229960002646 scopolamine Drugs 0.000 description 5
- 239000006227 byproduct Substances 0.000 description 4
- 230000002035 prolonged effect Effects 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 208000024827 Alzheimer disease Diseases 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 230000006386 memory function Effects 0.000 description 3
- 235000016709 nutrition Nutrition 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 238000005303 weighing Methods 0.000 description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 241001596950 Larimichthys crocea Species 0.000 description 2
- YPIGGYHFMKJNKV-UHFFFAOYSA-N N-ethylglycine Chemical compound CC[NH2+]CC([O-])=O YPIGGYHFMKJNKV-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 230000007087 memory ability Effects 0.000 description 2
- 230000007334 memory performance Effects 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 210000001835 viscera Anatomy 0.000 description 2
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 235000019733 Fish meal Nutrition 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 206010036631 Presenile dementia Diseases 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000009189 diving Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000004626 essential fatty acids Nutrition 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000003337 fertilizer Substances 0.000 description 1
- 235000021323 fish oil Nutrition 0.000 description 1
- 239000004467 fishmeal Substances 0.000 description 1
- 239000005417 food ingredient Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 235000013376 functional food Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 230000009191 jumping Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000000050 nutritive effect Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 1
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11B—PRODUCING, e.g. BY PRESSING RAW MATERIALS OR BY EXTRACTION FROM WASTE MATERIALS, REFINING OR PRESERVING FATS, FATTY SUBSTANCES, e.g. LANOLIN, FATTY OILS OR WAXES; ESSENTIAL OILS; PERFUMES
- C11B1/00—Production of fats or fatty oils from raw materials
- C11B1/02—Pretreatment
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11B—PRODUCING, e.g. BY PRESSING RAW MATERIALS OR BY EXTRACTION FROM WASTE MATERIALS, REFINING OR PRESERVING FATS, FATTY SUBSTANCES, e.g. LANOLIN, FATTY OILS OR WAXES; ESSENTIAL OILS; PERFUMES
- C11B1/00—Production of fats or fatty oils from raw materials
- C11B1/10—Production of fats or fatty oils from raw materials by extracting
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11B—PRODUCING, e.g. BY PRESSING RAW MATERIALS OR BY EXTRACTION FROM WASTE MATERIALS, REFINING OR PRESERVING FATS, FATTY SUBSTANCES, e.g. LANOLIN, FATTY OILS OR WAXES; ESSENTIAL OILS; PERFUMES
- C11B9/00—Essential oils; Perfumes
- C11B9/02—Recovery or refining of essential oils from raw materials
- C11B9/025—Recovery by solvent extraction
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Zoology (AREA)
- Health & Medical Sciences (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
The invention provides a method for preparing fish roe essential oil and fish roe functional peptide, which comprises the steps of crushing fish roe to obtain fish roe powder, and performing subcritical fluid extraction on the fish roe powder by using an extracting agent; separating the extractant after extraction is finished, and recovering the fish roe essential oil; removing the extractant from the fish roe residues, adding trypsin and collagenase for enzymolysis to obtain an enzymolysis liquid, and centrifuging to obtain a supernatant; and (4) performing membrane filtration on the supernatant to obtain a filtrate, namely the fish roe functional peptide solution. The method can simultaneously extract the fish roe essential oil and the fish roe functional peptide, has simple steps and strong operability, is beneficial to high-valued utilization of resources by synchronous extraction, reduces the cost and enhances the product competitiveness.
Description
Technical Field
The invention belongs to the technical field of separation and purification, and particularly relates to a method for preparing fish roe essential oil and fish roe functional peptide.
Background
China is a big country for processing aquatic products, and a large amount of fish byproducts such as fish scales, fish heads, internal organs and fish roes are generated in the fish processing process. These by-products are mainly used for the production of fish oil, fish meal, fertilizers, pet food and fish feed. It is reported that by-products in the ocean are the best source of health care products and functional food ingredients. At present, the utilization of fish skin, viscera and the like is high in value, and the utilization of fish roes is rarely reported.
Roe is a very important by-product in fish processing industry, and is rich in essential amino acids and fatty acids with high quality. It has been reported that fish roe contains protein in an amount of about 50-85% by dry weight and fat in an amount of about 8-32% by dry weight. The roe essential oil is unsaturated fatty acid in roe, is rich in DHA and EPA, and has effects of reducing inflammation reaction, reducing blood fat, and preventing cardiovascular disease. The fish roe functional peptide is a functional peptide mixture with a certain molecular weight range obtained by hydrolyzing fish roe protein with protease, and mainly comprises small molecular peptides with the molecular weight less than 1000 Da. The fish roe functional peptide not only can supplement amino acids required in vivo, but also has various physiological activities. However, at present, the essential oil and the protein are respectively extracted from the fish roes, and the extraction method is complex, so that the extraction cost is high.
Disclosure of Invention
The invention aims to provide a method for preparing fish roe essential oil and fish roe functional peptide, thereby making up the defects of the prior art.
The method for preparing the fish roe essential oil and the fish roe functional peptide comprises the following steps:
1) crushing: crushing the fish roe to obtain fish roe powder;
2) subcritical extraction: performing subcritical fluid extraction on the roe powder prepared in the step 1) by using an extracting agent; separating the extractant after extraction is finished, and recovering the fish roe essential oil;
the extractant is an extractant which is allowed to be used in the food industry such as butane and the like;
the extraction is carried out for 45min at the temperature of 45 DEG C
3) Enzymolysis: removing the extractant from the fish roe residues in the step 2), adding trypsin and collagenase for enzymolysis to obtain an enzymolysis liquid, and centrifuging to obtain a supernatant;
wherein the adding amount ratio of the trypsin to the collagenase in the homogenate is 1: 50-5: 1;
preferably, the enzyme activity ratio of the trypsin to the collagenase is 1: 10;
one of the enzymolysis conditions is enzymolysis for 3 to 5 hours at the temperature of between 35 and 55 ℃;
the rotation speed of the centrifugation is 6000-12000 rpm;
4) membrane filtration: and (3) performing membrane filtration on the supernatant prepared in the step 3), and obtaining a filtrate, namely the fish roe functional peptide solution.
The membrane separation in the step 4) is performed by using a 3500Da membrane, and then using a 360Da membrane.
The method can simultaneously extract the fish roe essential oil and the fish roe functional peptide, has simple steps and strong operability, is beneficial to high-valued utilization of resources by synchronous extraction, reduces the cost and enhances the product competitiveness.
Drawings
FIG. 1: a graph of a standard for polypeptide molecular weight;
FIG. 2: molecular weight distribution of the fish roe functional peptide.
Detailed Description
The present invention will be described in detail with reference to examples.
Example 1:
weighing 100g of dried yellow croaker roe, crushing by using a crusher, putting the crushed yellow croaker roe into a filter cloth bag, putting the filter cloth bag into a subcritical fluid extraction laboratory complete equipment extraction tank, adding butane into the filter cloth bag to submerge the filter cloth bag, extracting for 45min at the temperature of 45 ℃, separating an extracting agent, and recovering roe essential oil, wherein the yield is 19.87%. Removing butane from the roe residues, adding 1000ml of distilled water, adding 3g of trypsin and collagenase (enzyme activity ratio of 1:10), carrying out enzymolysis for 5h at 50 ℃, heating to 90 ℃ to inactivate enzyme after the enzymolysis is finished, centrifuging the enzymolysis liquid, collecting supernatant, separating the supernatant by using a membrane filter instrument to obtain a roe functional peptide solution of 360Da-3500Da, concentrating the solution to 1/10 of the original volume, and carrying out spray drying to obtain 30.98g of roe functional peptide, wherein the yield is 30.98%.
Example 2:
weighing 500g of dried roe, crushing by using a crusher, putting the crushed roe into a filter cloth bag, putting the filter cloth bag into an extraction tank of subcritical fluid extraction laboratory complete equipment, adding butane to submerge the filter cloth bag, extracting for 45min at the temperature of 45 ℃, separating an extracting agent, and recovering roe essential oil, wherein the yield is 20.37%. Removing butane from the roe residues, adding 1000ml of distilled water, adding 20g of trypsin and collagenase (enzyme activity ratio of 1:10), carrying out enzymolysis for 5h at 50 ℃, heating to 90 ℃ to inactivate enzyme after the enzymolysis is finished, centrifuging the enzymolysis liquid, collecting supernatant, separating the supernatant by using a membrane filter instrument to obtain a roe functional peptide solution of 360Da-3500Da, concentrating the solution to 1/10 of the original volume, and carrying out vacuum reduced pressure drying to obtain 137.72g of roe functional peptide, wherein the yield is 27.54%.
Example 3:
weighing 1000g of dried roe, crushing by using a crusher, putting the crushed roe into a filter cloth bag, putting the filter cloth bag into an extraction tank of subcritical fluid extraction laboratory complete equipment, adding butane to submerge the filter cloth bag, extracting for 45min at the temperature of 45 ℃, separating an extracting agent, and recovering roe essential oil, wherein the yield is 22.19%. Removing butane from the roe residues, adding 1000ml of distilled water, adding 30g of trypsin and collagenase (enzyme activity ratio of 1:10), carrying out enzymolysis for 5h at 50 ℃, heating to 90 ℃ to inactivate enzyme after the enzymolysis is finished, centrifuging the enzymolysis liquid, collecting supernatant, separating the supernatant by using a membrane filter instrument to obtain a roe functional peptide solution of 360Da-3500Da, concentrating the solution to 1/10 of the original volume, and carrying out freeze drying to obtain 263.31g of roe functional peptide, wherein the yield is 26.33%.
Example 4: research on fish roe essential oil and fish roe functional peptide
Determination of DHA and EPA contents in fish roe essential oil
According to the first method in the national standard (GB5009.168-2016), DHA and EPA in the roe essential oil of example 1 are detected, and the experimental result shows that the DHA content (g/100g) and the EPA content (g/100g) in the roe essential oil are respectively 13.4 and 4.35.
II, analyzing the molecular weight distribution of the fish roe functional peptide
The work of preparing the fish roe in the example 1 is determined according to the method of the national standard (GB/T22729-As shown in FIG. 1, the molecular weight of the active peptide is determined by using cytochrome C (12384Da), aprotinin (6512Da), bacitranase (1423Da), ethyl-casein-arginine (451Da) and ethyl-glycine (189Da) as standard substances, and establishing a standard curve to obtain a standard curve of retention time and molecular weight logarithm value, wherein the equation is y-0.2678 x +7.4913(R is-0.2678 x + 7.4913)20.974). According to the method of the standard curve, the molecular weight distribution of the fish roe functional peptide is analyzed, as shown in figure 2, the fish roe functional peptide with the molecular weight of less than 3500Da accounts for 90.34%.
Third, analysis of nutritive value of fish roe functional peptide
Nutritional value analysis was performed on the functional peptide of fish roe prepared in example 1.
① Essential Amino Acid (EAA) content to total amino acid amount (TAA) the ratio (E/N) of essential amino acids to non-essential amino acids (NEAA) is calculated as follows:
② amino acid evaluation index according to WHO/FAO/UNU 1985 recommended amino acid scoring mode[5]The adult group scoring mode was selected to calculate the essential Amino Acid Score (AAS) and Chemical Score (CS) in roe functional peptides according to the following formula.
The lowest overall tryptophan score among the functional fish roe peptides, which is the first limiting amino acid of the functional fish roe peptides, is obtained from table 1. WHO/FAO/UNU recommended the AAS of adults to be 100, i.e., the closer AAS and CS are to 100, the higher the nutritional value of the tested protein sample is. Except tryptophan, the AAS of other amino acids in the fish roe functional peptide is higher than 100, which shows that the fish roe active peptide has higher nutritional value.
TABLE 1 evaluation index of fish roe functional peptide amino acid
The results of the examination of the functional peptides prepared in examples 2 and 3 were similar to those of example 1, indicating that the prepared functional peptides of fish roe had similar effects.
Fourthly, the fish roe functional peptide improves the memory function
The fish roe functional peptide prepared in example 1 was evaluated for improving memory function.
4.1 Effect of functional peptide of roe on escape latency and number of times of platform crossing of rat with scopolamine induced dysmnesia
The water maze experiment result shows that the escape latency of rats in the model group is obviously prolonged compared with that of the control group, the escape latency of the high-dose group of the fish roe functional peptide is obviously smaller than that of the model group (P is less than 0.01) compared with that of the model group, and the escape latency of the medium-dose group is smaller than that of the model group (P is less than 0.05). The platform is removed on the 5 th day of the experiment, the space exploration capacity of each group of rats is observed, and the result shows that the number of times of crossing the platform is obviously reduced (P <01) when the rats in the model group are compared with the rats in the control group, which indicates that the learning and memory capacity is declined; compared with the model group, the times of crossing the platform of the high-dose group of the fish roe functional peptide are increased (P is less than 0.01), and the times of crossing the platform of the medium-dose group and the low-dose group are higher than those of the model group, but the statistical significance is avoided, so that the treatment group can improve the memory capacity of the rat with the scopolamine induced dysmnesia (Table 2).
Table 2: influence of roe functional peptide on avoiding latency and cross-platform times of AD rats (x soil s)
Note: p <005 compared to model group (scopolamine).
2.2 Effect of the functional peptide of roe on learning and memory ability of rat with presenile dementia caused by scopolamine
As shown in table 3, in the study result experiment, compared with the control group, the response time of the rat is significantly prolonged, the number of errors is significantly increased, which indicates that the study result of the mouse is reduced, and the difference has statistical significance (P < 0.01). Compared with the model group, the treatment groups have shorter response time, less error times and statistical significance of difference (P < 0.01). Compared with the positive drug group, the high-dose group has the advantages that the reaction time is shortened, the error frequency is increased, the difference has statistical significance (P <0.05), compared with the low-dose group, the reaction time is obviously shortened, the error frequency is reduced, the statistical significance (P <0.05) is realized, the high-dose group and the low-dose group show that the treatment groups can improve the study capacity of the platform jumping experiment of the Alzheimer's disease rats, and the fish roe functional peptide is in a remarkable dose-effect relationship in the aspect of improving the latency time. In the memory capacity experiment, compared with a control group, the latency time of a rat is obviously shortened, the error frequency is obviously increased, the memory performance is reduced, and the difference has statistical significance (P is less than 0.01); compared with the model group, the treatment groups have prolonged latency and reduced error frequency, and the difference has statistical significance (P <0.01), compared with the positive drug group, the high dose group has prolonged latency and obviously reduced error frequency, the difference has statistical significance (P <005), compared with the low dose group, the high dose group has obviously reduced error frequency, but the difference has no statistical significance.
Table 3: comparison table of learning and memory ability of rats in each group (x + -s)
Note: p <0.05 compared to model group (scopolamine).
The experimental results show that each treatment group can improve the diving platform memory performance of the Alzheimer's disease rats and has a dose-effect relationship trend in increasing the latent time.
The function of the fish roe functional peptides prepared in other examples in the specification of the invention is detected, and the fish roe functional peptides prepared by the invention have similar effect of improving the memory function.
Claims (9)
1. A method for preparing fish roe essential oil and fish roe functional peptide, which comprises the following steps:
1) crushing: crushing the fish roe to obtain fish roe powder;
2) subcritical extraction: performing subcritical fluid extraction on the roe powder prepared in the step 1) by using an extracting agent; separating the extractant after extraction is finished, and recovering the fish roe essential oil;
3) enzymolysis: removing the extractant from the fish roe residues in the step 2), adding trypsin and collagenase for enzymolysis to obtain an enzymolysis liquid, and centrifuging to obtain a supernatant;
4) membrane filtration: and (3) performing membrane filtration on the supernatant prepared in the step 3), and obtaining a filtrate, namely the fish roe functional peptide solution.
2. The method of claim 1, wherein the extraction in 2) is at 45 ℃.
3. The method of claim 1, wherein the extractant is an extractant used in the food industry.
4. The method of claim 1 or 3, wherein the extractant is butane.
5. The method of claim 1, wherein the trypsin and collagenase in 3) are added in a ratio of 1:50 to 5:1 in the homogenate.
6. The method of claim 1, wherein the trypsin and collagenase in 3) are added in a ratio of 1:10 in the homogenate.
7. The method as claimed in claim 1, wherein the enzymolysis condition in 3) is enzymolysis at 35-55 ℃ for 3-5 h.
8. The method as claimed in claim 1, wherein the rotation speed of the centrifugation in 3) is 6000-12000 rpm.
9. The method of claim 1, wherein the membrane separation in 4) is a separation with 3500Da membrane, followed by 360Da membrane.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202010336233.4A CN111484893A (en) | 2020-04-24 | 2020-04-24 | Method for synchronously preparing fish roe essential oil and fish roe functional peptide |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202010336233.4A CN111484893A (en) | 2020-04-24 | 2020-04-24 | Method for synchronously preparing fish roe essential oil and fish roe functional peptide |
Publications (1)
Publication Number | Publication Date |
---|---|
CN111484893A true CN111484893A (en) | 2020-08-04 |
Family
ID=71791778
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN202010336233.4A Pending CN111484893A (en) | 2020-04-24 | 2020-04-24 | Method for synchronously preparing fish roe essential oil and fish roe functional peptide |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN111484893A (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN112190530A (en) * | 2020-10-30 | 2021-01-08 | 深圳市洛奇机电科技有限公司 | Preparation method of cod roe essence mask |
CN114317652A (en) * | 2021-12-16 | 2022-04-12 | 中国科学院兰州化学物理研究所 | Method for separating and purifying polypeptide with memory improving function from fish roe polypeptide by using porous polymer separation material |
Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN102839207A (en) * | 2012-09-17 | 2012-12-26 | 温州大学 | Method for preparing collagen peptide from fish scales |
CN103409489A (en) * | 2013-08-15 | 2013-11-27 | 集美大学 | Preparation method for fish collagen antioxidant peptide |
CN103627759A (en) * | 2013-09-12 | 2014-03-12 | 郑州市中食农产品加工研究院 | Method for extracting and preparing active ingredients of fish roes |
CN106319014A (en) * | 2016-10-14 | 2017-01-11 | 浙江双屿生物股份有限公司 | Extracting method for micro-molecule deep-sea fish polypeptides |
-
2020
- 2020-04-24 CN CN202010336233.4A patent/CN111484893A/en active Pending
Patent Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN102839207A (en) * | 2012-09-17 | 2012-12-26 | 温州大学 | Method for preparing collagen peptide from fish scales |
CN103409489A (en) * | 2013-08-15 | 2013-11-27 | 集美大学 | Preparation method for fish collagen antioxidant peptide |
CN103627759A (en) * | 2013-09-12 | 2014-03-12 | 郑州市中食农产品加工研究院 | Method for extracting and preparing active ingredients of fish roes |
CN106319014A (en) * | 2016-10-14 | 2017-01-11 | 浙江双屿生物股份有限公司 | Extracting method for micro-molecule deep-sea fish polypeptides |
Non-Patent Citations (2)
Title |
---|
何贵山等: "飞鱼籽生物酶法脱囊衣技术研究", 《食品科技》 * |
魏鉴腾等: "酶解法制备鱼籽多肽的工艺研究", 《食品工业》 * |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN112190530A (en) * | 2020-10-30 | 2021-01-08 | 深圳市洛奇机电科技有限公司 | Preparation method of cod roe essence mask |
CN112190530B (en) * | 2020-10-30 | 2021-07-16 | 烟台新时代健康产业日化有限公司 | Preparation method of cod roe essence mask |
CN114317652A (en) * | 2021-12-16 | 2022-04-12 | 中国科学院兰州化学物理研究所 | Method for separating and purifying polypeptide with memory improving function from fish roe polypeptide by using porous polymer separation material |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Tian et al. | Ultrasonic-assisted extraction and antioxidant activity of polysaccharides recovered from white button mushroom (Agaricus bisporus) | |
CN105567774B (en) | A kind of oligomeric Gly-His-Lys of walnut and its preparation method and application | |
Zhu et al. | Extraction, structural and functional properties of Haematococcus pluvialis protein after pigment removal | |
CN105936927B (en) | Walnut oligopeptide and preparation process and application thereof | |
CN111484893A (en) | Method for synchronously preparing fish roe essential oil and fish roe functional peptide | |
CN106632605B (en) | Active peptide prepared from tuna leftovers and having liver injury repair effect | |
CN110498785A (en) | A kind of lycium ruthenicum anthocyanidin and preparation method thereof | |
CN108456244A (en) | Corn antioxidant active peptide and preparation method thereof | |
CN102613384B (en) | Method for preparing spiral seaweed polypeptide powder by using living spiral seaweeds | |
CN113845566B (en) | Walnut polypeptide for preventing Alzheimer's disease and application thereof | |
CN111455007B (en) | Polypeptide prepared from fish roe and used for improving memory function | |
CN103343154A (en) | Preparation of soybean anti-fatigue biological active peptide | |
CN103014108A (en) | Preparation method of corn oligopeptide | |
CN107177656A (en) | A kind of loach fish protein polypeptide and its application | |
CN113698454B (en) | Walnut meal acetylcholine esterase inhibitory peptide as well as preparation method and application thereof | |
CN103099248A (en) | Method for preparing oyster active component | |
CN104762283B (en) | Separation method, protease and its application of golden pomfret visceral protein enzyme | |
CN114517218A (en) | Sea-buckthorn oligopeptide powder and preparation method and application thereof | |
CN116375902A (en) | Grape residue polysaccharide for improving immune function and preparation method and application thereof | |
CN109548951A (en) | The extracting method of quinoa bran protein and its application in terms of food | |
CN114592024A (en) | Sheep placenta polypeptide and preparation method and application thereof | |
CN107125696A (en) | A kind of separation of chicken delicate flavour peptide and preparation method thereof | |
CN106244462A (en) | A kind of ganoderma lucidum mycelium liquid fermentation culture method | |
JP2001145472A (en) | Composition having fatty liver-suppressing activity fractionated from residual liquid of barley shochu liquor distillation and production of the same composition | |
CN105998091A (en) | Extraction method for triterpenoid substance of antrodia camphorata and extract |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PB01 | Publication | ||
PB01 | Publication | ||
SE01 | Entry into force of request for substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
WD01 | Invention patent application deemed withdrawn after publication | ||
WD01 | Invention patent application deemed withdrawn after publication |
Application publication date: 20200804 |