LU500718B1 - Method for preparing highly antioxidant black carp flesh anticancer peptide - Google Patents
Method for preparing highly antioxidant black carp flesh anticancer peptide Download PDFInfo
- Publication number
- LU500718B1 LU500718B1 LU500718A LU500718A LU500718B1 LU 500718 B1 LU500718 B1 LU 500718B1 LU 500718 A LU500718 A LU 500718A LU 500718 A LU500718 A LU 500718A LU 500718 B1 LU500718 B1 LU 500718B1
- Authority
- LU
- Luxembourg
- Prior art keywords
- flesh
- pretreatment liquid
- fish
- black carp
- preparing
- Prior art date
Links
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/04—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from fish or other sea animals
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/56—Materials from animals other than mammals
- A61K35/60—Fish, e.g. seahorses; Fish eggs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
- A61K38/012—Hydrolysed proteins; Derivatives thereof from animals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Veterinary Medicine (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Biochemistry (AREA)
- Polymers & Plastics (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Nutrition Science (AREA)
- Marine Sciences & Fisheries (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Organic Chemistry (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The present disclosure provides a method for preparing a highly antioxidant black carp flesh anticancer peptide. Using black carp flesh as a raw material, a first pretreatment liquid is prepared, the fish flesh is soaked in the first pretreatment liquid at room temperature for 2-5 h, and the fish flesh is washed with clean water after soaking; a second pretreatment liquid is prepared, washed fish flesh is soaked in the second pretreatment liquid at 50 ± 5°C for 1-2 h, soaked fish flesh is smashed into minced fish, the minced fish is mixed with purified water to prepare a minced fish suspension, and the minced fish suspension is subjected to two-step enzymatic hydrolysis with alkaline protease and compound protease to obtain the highly antioxidant black carp flesh anticancer peptide. The method for preparing a highly antioxidant anticancer peptide provided by the present disclosure is simple to operate, innocuous and harmless, easy to achieve, and capable of enriching anticancer peptide product categories, providing a new raw material for developing inexpensive anticancer products.
Description
METHOD FOR PREPARING HIGHLY ANTIOXIDANT BLACK CARP FLESH HUS00718
[01] The present disclosure belongs to the technical field of food processing, and particularly relates to a method for preparing a highly antioxidant black carp flesh anticancer peptide.
[02] Anticancer peptide is a bioactive peptide with antitumor activity, which achieves a killing effect on cancer cells by destroying the tumor cell membrane structure or inhibiting the proliferation and migration of cancer cells and the tumor angiogenesis, with a low toxic effect on normal cells.
[03] Black carp (Mylopharyngodon piceus), belonging to the genus Mylopharyngodon of the family Cyprinidae in the order Cypriniformes, is one of the seven major freshwater fishes in China. At present, research on black carp mainly focuses on rearing methods and control of fish diseases, but the utilization and deep processing of fish flesh have not been reported yet.
[04] The present disclosure provides a method for preparing a highly antioxidant black carp flesh anticancer peptide. Using black carp flesh as a raw material, a first pretreatment liquid is prepared, the fish flesh is soaked in the first pretreatment liquid at room temperature for 2-5 h, and the fish flesh is washed with clean water after soaking; a second pretreatment liquid is prepared, washed fish flesh is soaked in the second pretreatment liquid at 50 + 5°C for 1-2 h, soaked fish flesh is smashed into minced fish, the minced fish is mixed with purified water to prepare a minced fish suspension, and the minced fish suspension is subjected to two-step enzymatic hydrolysis with alkaline protease and compound protease to obtain the highly antioxidant black carp flesh anticancer peptide.
[05] The first pretreatment liquid is an aqueous solution of acetic acid and H:O>, where the acetic acid has a mass percentage of 5%-8%, and the H,O, has a mass percentage of 2%-3%;
[06] the second pretreatment liquid is an aqueous solution of tea-star anise extract complex and glucose.
[07] Further, the second pretreatment liquid may be prepared as follows:
[08] step 1, mixing green tea leaves with star anise, grinding a resulting mixture into a powder, charging the powder into deionized water, heating to 90 + 5°C, holding, and extracting for 2-3 h; after extraction, air-cooling to room temperature, filtering to remove a solid phase, and 1 concentrating a liquid phase under reduced pressure; and HUS00718
[09] step 2, charging glucose into a filtrate concentrated under reduced pressure, stirring and mixing well to obtain the second pretreatment liquid.
[10] Further, the green tea leaves and the star anise may be mixed in a mass ratio of 10:(3-8); the mass of the deionized water added may be 6 times the mass of the powder; the liquid phase may be concentrated to 1/3 of unconcentrated volume under reduced pressure.
[11] Further, the glucose in the second pretreatment liquid may have a mass percentage of 1%-2%.
[12] Further, the preparation method may include the following specific steps:
[13] 1. Raw material pretreatment: fresh black carp is slaughtered, scaled, and skinned to separate fish flesh; the fish flesh is soaked in the first pretreatment liquid at room temperature for 2-5 h, and the fish flesh is washed with clean water after soaking; a second pretreatment liquid is prepared, washed fish flesh is soaked in the second pretreatment liquid at 50 + 5°C for 1-2 h, and soaked fish flesh is smashed into minced fish;
[14] 2. One-step enzymatic hydrolysis: the minced fish is dispersed in purified water to prepare a minced fish suspension, and the suspension is subjected to one-step enzymatic hydrolysis with alkaline protease; after the enzymatic hydrolysis, the enzyme is inactivated, and an enzymatic hydrolysate is subjected to centrifugal separation; a supernatant is collected and freeze-dried to obtain a freeze-dried enzymatic hydrolysate; and
[15] 3. Two-step enzymatic hydrolysis: the freeze-dried enzymatic hydrolysate is formulated into an enzymatic hydrolysate solution, two-step enzymatic hydrolysis is conducted by using a compound protease; after the enzymatic hydrolysis, the enzyme is inactivated, and a supernatant is obtained by centrifugation, namely, the highly antioxidant black carp flesh anticancer peptide is obtained.
[16] Further, in step 2, the minced fish in the minced fish suspension may have mass fraction of 10%; the amount of the alkaline protease added may be 8,000 U/g; one-step enzymatic hydrolysis conditions may be: pH 8.00, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h, with pH adjusted to 8.00 with a 0.1 mol/L NaOH solution.
[17] Further, in step 3, the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution may be 1-5 g/mL; the amount of the compound protease added may be 2,000-10,000 U/g; two-step enzymatic hydrolysis conditions may be: pH 6-9, temperature 40-65°C, and enzymatic hydrolysis time 1-5 h.
[18] Further, parameters for the two-step enzymatic hydrolysis may be as follows: the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution may be 2.0 g/mL; the amount of the compound protease added may be 6,000 U/g; the pH may be 8.0, the 2 temperature may be 55.00°C, and the time may be 3 h. HUS00718
[19] Therefore, according to the above technical solution, the present disclosure has the following beneficial effects: in the present disclosure, black carp flesh as a raw material is smashed into minced fish for pretreatment, one-step enzymatic hydrolysis is conducted with alkaline protease, and enzymatic hydrolysate is subjected to two-step enzymatic hydrolysis with compound protease to enhance the antioxidant activity of bioactive peptide. The method for preparing a highly antioxidant anticancer peptide provided by the present disclosure is simple to operate, innocuous and harmless, and easy to achieve.
[20] Detailed descriptions will be made below in conjunction with the examples:
[21] Examples 1 to 9
[22] It was experimentally found that process parameters for the second step of enzymatic hydrolysis had a large effect on the antioxidant activity of the product. Therefore, the following orthogonal test was designed. Conditions for the second step of enzymatic hydrolysis with compound protease were optimized by changing parameters for two-step enzymatic hydrolysis. Nine groups of tests were designed, and the orthogonal test was optimized regarding the temperature, time and pH in two-step enzymatic hydrolysis. Other processes of the nine groups of tests, such as raw material pretreatment and one-step enzymatic hydrolysis method, were identical. Steps were as follows:
[23] 1. Raw material pretreatment: fresh black carp was slaughtered, scaled, and skinned to separate fish flesh; a first pretreatment liquid was prepared, the fish flesh was soaked in the first pretreatment liquid at room temperature for 2 h, and the fish flesh was washed with clean water after soaking; a second pretreatment liquid was prepared, washed fish flesh was soaked in the second pretreatment liquid at 50 + 5°C for 1 h, and soaked fish flesh was smashed into minced fish; herein, the first pretreatment liquid was an aqueous solution of acetic acid and H>O,, where the acetic acid had a mass percentage of 6%, and the HO: has a mass percentage of 2%; the second pretreatment liquid was prepared as follows: step 1, green tea leaves were mixed with star anise in a mass ratio of 10:5, the resulting mixture was ground into a powder, the powder was charged into deionized water (the mass of the deionized water was 6 times the mass of the powder), heated to 90 + 5°C, held, and extracted for 2 h; after extraction, the mixture was air-cooled to room temperature and filtered to remove a solid phase, and a liquid phase was concentrated to 1/3 of unconcentrated volume under reduced pressure; and step 2, glucose was charged into a filtrate concentrated under reduced pressure, stirred and mixed well to obtain the second pretreatment liquid, where the glucose in the second pretreatment liquid had a mass 3 percentage of 2%. HUS00718
[24] 2. One-step enzymatic hydrolysis: the minced fish was dispersed in purified water to prepare a minced fish suspension, where the minced fish in the minced fish suspension had a mass fraction of 10%; the suspension was subjected to one-step enzymatic hydrolysis with alkaline protease, where the amount of the alkaline protease added was 8,000 U/g; one-step enzymatic hydrolysis conditions were: pH 8.00, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h, with pH adjusted to 8.00 with a 0.1 mol/L NaOH solution. After the enzymatic hydrolysis, the enzyme was inactivated, and an enzymatic hydrolysate was subjected to centrifugal separation; a supernatant was collected and freeze-dried to obtain a freeze-dried enzymatic hydrolysate.
[25] 3. Two-step enzymatic hydrolysis: the freeze-dried enzymatic hydrolysate was formulated into an enzymatic hydrolysate solution, where the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution was 2 g/mL; two-step enzymatic hydrolysis was conducted by using a compound protease, where the amount of the compound protease added was 6,000 U/g. Parameters of two-step enzymatic hydrolysis conditions in each test group are shown in Table 1. After the enzymatic hydrolysis, the enzyme was inactivated, and a supernatant was obtained by centrifugation, namely, the highly antioxidant black carp flesh anticancer peptide was obtained.
[26] Cytotoxicity assay
[27] Cancer cells at logarithmic growth phase were inoculated onto a 96-well cell culture plate, which were only inoculated inside the cell culture plate in order to prevent the edge effect. Phosphate buffered saline (PBS) was charged outside to prevent cells from water loss. When adding to the cell culture plate, there were approximately 5,000 cells per well, which were cultured in 5% CO» at 37°C for 24 h; the residual culture medium was removed, and the cells were washed with PBS twice. Herein, 100 uL each of sample-containing culture medium (As) was added to experimental cells, and 100 uL each of culture medium (Ac) was added to control wells. The cell culture plate was cultured in 5% CO» at 37°C for 24 h, and then the plate was tested. The residual culture medium was removed from the plate, the cells were washed thrice with PBS, mixed with 100 uL of 5% CCK-8 solution, and cultured at 37°C for 3 h; the absorbance of the cell culture medium in each well was read at 450 nm. The absorbance (Ab) of the 5% CCK-8 solution under the same culture conditions was used as a ground color. The cell viability was calculated according to the following formula:.
[28] Cell viability = À 7 #s x 100%.
[29] Table 1 Test design solutions and results 4
"Experimental pH Temperature Time (h) ICs value of DPPH radical 17900718 group pH (°C) Time scavenging activity 1 8 45 2 13.20 2 8 50 3 10.45 3 8 55 4 11.37 4 8.5 45 3 12.17
8.5 50 4 11.99 6 8.5 55 2 14.75 7 9 45 4 13.54 8 9 50 2 14.41 9 9 55 3 13.77 K1 35.02 38.91 42.36 K2 38.91 36.85 36.39 K3 41.72 39.89 36.90 k1 11.67 12.97 14.12 k2 12.97 12.28 12.13 k3 13.91 13.30 12.30 R 2.23 1.01 1.99
[30] According to the orthogonal test results, the optimal conditions for two-step enzymatic hydrolysis with compound protease were obtained as follows: the pH was 8.0, temperature was 50°C, and time was 3 h.
[31] Example 10
[32] A method for preparing a highly antioxidant black carp flesh anticancer peptide included the following steps:
[33] 1. Raw material pretreatment: fresh black carp was slaughtered, scaled, and skinned to separate fish flesh; a first pretreatment liquid was prepared, the fish flesh was soaked in the first pretreatment liquid at room temperature for 2 h, and the fish flesh was washed with clean water after soaking; a second pretreatment liquid was prepared, washed fish flesh was soaked in the second pretreatment liquid at 50 + 5°C for 1 h, and soaked fish flesh was smashed into minced fish; herein, the first pretreatment liquid was an aqueous solution of acetic acid and H2O2, where the acetic acid had a mass percentage of 6%, and the H,O, has a mass percentage of 2%; the second pretreatment liquid was prepared as follows: step 1, green tea leaves were mixed with star anise in a mass ratio of 10:5, the resulting mixture was ground into a powder, the powder was charged into deionized water (the mass of the deionized water was 6 times the mass of the powder), heated to 90 + 5°C, held, and extracted for 2 h; after extraction, the mixture was air-cooled to room temperature and filtered to remove a solid phase, and a liquid phase was concentrated to 1/3 of unconcentrated volume under reduced pressure; and step 2, glucose was 5 charged into a filtrate concentrated under reduced pressure, stirred and mixed well to obtain the 200718 second pretreatment liquid, where the glucose in the second pretreatment liquid had a mass percentage of 2%.
[34] 2. One-step enzymatic hydrolysis: the minced fish was dispersed in purified water to prepare a minced fish suspension, where the minced fish in the minced fish suspension had a mass fraction of 10%; the suspension was subjected to one-step enzymatic hydrolysis with alkaline protease, where the amount of the alkaline protease added was 8,000 U/g; one-step enzymatic hydrolysis conditions were: pH 8.00, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h, with pH adjusted to 8.00 with a 0.1 mol/L NaOH solution. After the enzymatic hydrolysis, the enzyme was inactivated, and an enzymatic hydrolysate was subjected to centrifugal separation; a supernatant was collected and freeze-dried to obtain a freeze-dried enzymatic hydrolysate.
[35] 3. Two-step enzymatic hydrolysis: the freeze-dried enzymatic hydrolysate was formulated into an enzymatic hydrolysate solution, where the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution was 2 g/mL; two-step enzymatic hydrolysis was conducted by using a compound protease, where the amount of the compound protease added was 6,000 U/g. Two-step enzymatic hydrolysis conditions were as follows: pH 8.0, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 3 h. After the enzymatic hydrolysis, the enzyme was inactivated, and a supernatant was obtained by centrifugation, namely, the highly antioxidant black carp flesh anticancer peptide in this example was obtained.
[36] Comparative Example 1
[37] A method for preparing a highly antioxidant black carp flesh anticancer peptide included the following steps:
[38] 1. Raw material pretreatment: fresh black carp was slaughtered, scaled, and skinned to separate fish flesh; the fish flesh was washed with deionized water and smashed into minced fish.
[39] 2. One-step enzymatic hydrolysis: the minced fish was dispersed in purified water to prepare a minced fish suspension, where the minced fish in the minced fish suspension had a mass fraction of 10%; the suspension was subjected to one-step enzymatic hydrolysis with alkaline protease, where the amount of the alkaline protease added was 8,000 U/g; one-step enzymatic hydrolysis conditions were: pH 8.00, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h, with pH adjusted to 8.00 with a 0.1 mol/L NaOH solution. After the enzymatic hydrolysis, the enzyme was inactivated, and an enzymatic hydrolysate was subjected to centrifugal separation; a supernatant was collected and freeze-dried to obtain a freeze-dried enzymatic hydrolysate.
6
[40] 3. Two-step enzymatic hydrolysis: the freeze-dried enzymatic hydrolysate was 0718 formulated into an enzymatic hydrolysate solution, where the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution was 2 g/mL; two-step enzymatic hydrolysis was conducted by using a compound protease, where the amount of the compound protease added was 6,000 U/g. Two-step enzymatic hydrolysis conditions were as follows: pH 8.0, enzymatic hydrolysis temperature 45°C, and enzymatic hydrolysis time 2 h. After the enzymatic hydrolysis, the enzyme was inactivated, and a supernatant was obtained by centrifugation, namely, the highly antioxidant black carp flesh anticancer peptide in this comparative example was obtained.
[41] Comparative Example 2
[42] A method for preparing a highly antioxidant black carp flesh anticancer peptide included the following steps:
[43] 1. Raw material pretreatment: fresh black carp was slaughtered, scaled, and skinned to separate fish flesh; a pretreatment liquid was prepared, the fish flesh was soaked in the pretreatment liquid at room temperature for 2 h, and the fish flesh was washed with clean water after soaking; the fish flesh was removed and smashed into minced fish; herein, the pretreatment liquid was an aqueous solution of acetic acid and H>O,, where the acetic acid had a mass percentage of 6%, and the H,O» has a mass percentage of 2%.
[44] 2. One-step enzymatic hydrolysis: the minced fish was dispersed in purified water to prepare a minced fish suspension, where the minced fish in the minced fish suspension had a mass fraction of 10%; the suspension was subjected to one-step enzymatic hydrolysis with alkaline protease, where the amount of the alkaline protease added was 8,000 U/g; one-step enzymatic hydrolysis conditions were: pH 8.00, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h, with pH adjusted to 8.00 with a 0.1 mol/L NaOH solution. After the enzymatic hydrolysis, the enzyme was inactivated, and an enzymatic hydrolysate was subjected to centrifugal separation; a supernatant was collected and freeze-dried to obtain a freeze-dried enzymatic hydrolysate.
[45] 3. Two-step enzymatic hydrolysis: the freeze-dried enzymatic hydrolysate was formulated into an enzymatic hydrolysate solution, where the ratio of the freeze-dried enzymatic hydrolysate in the enzymatic hydrolysate solution was 2 g/mL; two-step enzymatic hydrolysis was conducted by using a compound protease, where the amount of the compound protease added was 6,000 U/g. Two-step enzymatic hydrolysis conditions were as follows: pH 8.5, enzymatic hydrolysis temperature 50°C, and enzymatic hydrolysis time 4 h. After the enzymatic hydrolysis, the enzyme was inactivated, and a supernatant was obtained by centrifugation, namely, the highly antioxidant black carp flesh anticancer peptide in this comparative example 7 was obtained. HUS00718
[46] The results of the DPPH radical scavenging activity and HepG2 cell inhibition rate tested for the highly antioxidant black anticancer peptides prepared in Example 10 and Comparative Examples 1 and 2 are shown in Table 2.
[47] Table? activity (mg/mL rate
[48] In the above, the technical solution provided by the present disclosure is described in detail. A person of ordinary skill in the art may make a change in the specific implementation and application range of the present disclosure according to the concept of the examples. To sum up, the content of this specification should not be constructed as a limit to the present disclosure.
8
Claims (4)
1. A method for preparing a highly antioxidant black carp flesh anticancer peptide, comprising: preparing a first pretreatment liquid using black carp flesh as a raw material, soaking fish flesh in the first pretreatment liquid at room temperature for 2-5 h, and washing the fish flesh with clean water after soaking; preparing a second pretreatment liquid, soaking the washed fish flesh in the second pretreatment liquid at 50 + 5°C for 1-2 h, smashing the soaked fish flesh into minced fish, mixing the minced fish with purified water to prepare a minced fish suspension, and subjecting the minced fish suspension to two-step enzymatic hydrolysis with alkaline protease and compound protease to obtain the highly antioxidant black carp flesh anticancer peptide; wherein the first pretreatment liquid is an aqueous solution of acetic acid and H,O, wherein the acetic acid has a mass percentage of 5%-8%, and the H,O, has a mass percentage of 2%-3%; and the second pretreatment liquid is an aqueous solution of tea-star anise extract complex and glucose.
2. The method for preparing a highly antioxidant black carp flesh anticancer peptide according to claim 1, wherein the second pretreatment liquid is prepared as follows: step 1, mixing green tea leaves with star anise, grinding a resulting mixture into a powder, charging the powder into deionized water, heating to 90 + 5°C, holding, and extracting for 2-3 h; after extraction, air-cooling to room temperature, filtering to remove a solid phase, and concentrating a liquid phase under reduced pressure; and step 2, charging glucose into a filtrate concentrated under reduced pressure, stirring and mixing well to obtain the second pretreatment liquid.
3. The method for preparing a highly antioxidant black carp flesh anticancer peptide according to claim 2, wherein the green tea leaves and the star anise are mixed in a mass ratio of 10:(3-8); the mass of the deionized water added is 6 times the mass of the powder; the liquid phase is concentrated to 1/3 of unconcentrated volume under reduced pressure.
4. The method for preparing a highly antioxidant black carp flesh anticancer peptide according to claim 2, wherein the glucose in the second pretreatment liquid has a mass percentage of 1%-2%.
9
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| LU500718A LU500718B1 (en) | 2021-10-11 | 2021-10-11 | Method for preparing highly antioxidant black carp flesh anticancer peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| LU500718A LU500718B1 (en) | 2021-10-11 | 2021-10-11 | Method for preparing highly antioxidant black carp flesh anticancer peptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| LU500718B1 true LU500718B1 (en) | 2022-04-11 |
Family
ID=81127807
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| LU500718A LU500718B1 (en) | 2021-10-11 | 2021-10-11 | Method for preparing highly antioxidant black carp flesh anticancer peptide |
Country Status (1)
| Country | Link |
|---|---|
| LU (1) | LU500718B1 (en) |
-
2021
- 2021-10-11 LU LU500718A patent/LU500718B1/en active IP Right Grant
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN111647072B (en) | Antioxidant peptide and preparation method and application thereof | |
| CN108129552B (en) | Sea cucumber-derived antioxidant active peptide and extraction method | |
| CN108244402B (en) | Protein source heavy metal removing agent suitable for mussels and preparation method thereof | |
| US20210000136A1 (en) | Process to improve enzyme hydrolysis and resultant protein flavor and bio-activity of fish offcuts | |
| CN107164447A (en) | A kind of method that utilization cod processing accessory substance prepares anti-oxidation peptide | |
| US20220135616A1 (en) | Method for extracting useful substances from shrimp shells | |
| AU2021105562A4 (en) | Preparation Method of Tilapia Protein Peptide with Antioxidant and Antifatigue Activities | |
| CN104382953A (en) | Extraction method of melanin in black fungi | |
| CN110746515A (en) | Lycium barbarum polysaccharide, lycium barbarum red element and lycium barbarum polypeptide prepared by synchronous separation and preparation method thereof | |
| KR101377586B1 (en) | Method for producing fermented inonotus obliquus with increased antioxidant activity and total phenolic compounds by the solid-state fermentation | |
| CN110862328B (en) | Preparation method of L-carnitine amino acid eutectic solvent and application of L-carnitine amino acid eutectic solvent in polyphenol extraction | |
| CN112245342B (en) | Ginseng series skin care extract and preparation method and application thereof | |
| LU500718B1 (en) | Method for preparing highly antioxidant black carp flesh anticancer peptide | |
| CN115671189B (en) | Method for combined extraction of tea polyphenol and tea seleno peptide from tea | |
| CN110713450A (en) | Astaxanthin extraction method based on haematococcus pluvialis | |
| CN112795614B (en) | Composite polypeptide extract with blood glucose and lipid reducing activities and application thereof | |
| CN113957113A (en) | Oyster oligopeptide and preparation method thereof | |
| CN108040939B (en) | Temporary rearing method for controlling heavy metal enrichment of mussels | |
| CN111374219A (en) | Preparation method of black carp fish high-oxidation-resistance anticancer peptide | |
| CN104337837A (en) | Anti-lung cancer application of ruditapes philippinarum enzymatic hydrolysate | |
| US20230141130A1 (en) | Phenolic stabilized fruit juice and preparation method thereof | |
| AU2021104232A4 (en) | Application of sanghuangporus sanghuang fermentation broth polysaccharides in medicaments of anti-avian influenza virus | |
| CN105002245A (en) | Tuna dark meat protein antioxidative iron-chelating peptide preparation method | |
| CN117844871A (en) | Peony extract, product containing peony extract, preparation method and application of peony extract | |
| CN116458593A (en) | Preparation method of food preservative |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Patent granted |
Effective date: 20220411 |