CN114107419A - Cassava leaf polypeptide and preparation method and application thereof - Google Patents
Cassava leaf polypeptide and preparation method and application thereof Download PDFInfo
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- CN114107419A CN114107419A CN202111480152.2A CN202111480152A CN114107419A CN 114107419 A CN114107419 A CN 114107419A CN 202111480152 A CN202111480152 A CN 202111480152A CN 114107419 A CN114107419 A CN 114107419A
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- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
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Abstract
The invention provides a preparation method of cassava leaf polypeptide, which comprises the following steps: s1, preprocessing, and extracting total protein of cassava leaves; s2, carrying out enzymolysis on the cassava leaf total protein by using protease to obtain an enzymolysis liquid; s3, carrying out ultrafiltration on the enzymolysis liquid, and collecting polypeptide liquid with the molecular weight lower than 3 kDa; s4, carrying out microwave heating on the obtained polypeptide liquid for 30-40S to obtain the cassava leaf polypeptide. Compared with the prior art, the cassava leaf polypeptide prepared by the invention has high conversion rate and strong antioxidant effect, so that the cassava leaf polypeptide can be added into beverages or functional nutritional foods to improve the antioxidant health-care effect; meanwhile, the cassava leaf polypeptide is a small molecular polypeptide with the molecular weight less than 3kDa, and is beneficial to processing and utilization in industries such as food, cosmetics and the like.
Description
Technical Field
The invention relates to the technical field of bioengineering, and particularly relates to cassava leaf polypeptide and a preparation method and application thereof.
Background
Cassava (Manihot esculenta Crantz) is a plant of cassava of Euphorbiaceae, originates from tropical America, is a beautiful name of 'underground granary', 'starch king' and 'energy crop', is one of three potato crops in the world, and is an important food and feed crop and a renewable energy source-alcohol main raw material in tropical and subtropical regions. At present, more than 5 hundred million people in the world live with cassava as the main food.
Cassava is mainly distributed in Brazil, Mexico, Nigeria, Borlivia, Thailand, Columbia, Indonesia, and the like. The introduction and cultivation of China in the 20 th century in 19 th century now has been widely distributed in south China, the largest area of cultivation in Guangdong and Guangxi, Fujian and Taiwan, and a small amount of cultivation in Yunnan, Guizhou, Sichuan, Hunan, Jiangxi provinces.
At present, most of the major cassava producing countries in the world only stay in the aspect of cassava starch in comprehensive utilization and development, and have few comprehensive utilization and development researches on a large amount of byproducts generated in the cassava production process, such as cassava stems, fresh cassava leaves, cassava residues, cassava peels and other wastes, so that the byproducts are randomly discarded, the waste of resources is caused, and the pollution to the ecological environment is also caused. According to the experimental detection result, the protein content of the fresh cassava leaves is generally between 4.0 and 11.8 percent, the highest content can reach 11.8 percent, the protein content of the fresh cassava leaves is generally between 20.6 and 36.4 percent, the highest content can reach 39.9 percent, the content of amino acid is 8.42 to 9.4 percent, the average content of essential amino acid is 4.21 percent, the essential amino acid accounts for about 50 percent, other main amino acids are quite rich except methionine which is lower than the critical level, and carotene, crude fiber, crude protein, calcium, vitamins and trace elements are all rich, can be compared with most of tropical leguminous pasture, even better, are similar to alfalfa grass in rank, and can be used for breeding grass carp, goats and castor silkworms. Because the cassava leaf protein generally exists in a macromolecular structure form, the direct ingestion and digestion utilization rate of organisms is not high, the application range is not wide without deep processing, and the additional value is not high, so that a novel method for preparing the protein polypeptide in the cassava waste is developed, the waste is changed into valuable, rich peptide substances are provided for the industries of high-quality feed, food, medicine and health care products, and the method is beneficial to human beings.
With the release of the "healthy china 2030" program outline ", healthy diet is the mainstream of the current life. The polypeptide is an important raw material of health food, has various obvious physiological effects, is safe in source and free of side effect, and is widely applied to processing and utilizing of food and health care products. Plant-derived polypeptides such as soybean and wheat are the key points of the current application. Researches show that the cassava can generate rich polypeptide mixture through certain treatment, has obvious antioxidant function and wide application prospect. However, the cassava leaf polypeptide obtained by the existing preparation method is insufficient in purity or low in yield, and needs to be further improved.
Disclosure of Invention
The first aspect of the invention aims to provide a preparation method of cassava leaf polypeptide, which comprises the following steps:
s1, preprocessing, and extracting total protein of cassava leaves;
s2, carrying out enzymolysis on the cassava leaf total protein by using protease to obtain an enzymolysis liquid;
s3, carrying out ultrafiltration on the enzymolysis liquid, and collecting polypeptide liquid with the molecular weight lower than 3 kDa;
s4, carrying out microwave heating on the obtained polypeptide liquid for 30-40S to obtain the cassava leaf polypeptide.
In one or more embodiments, the step S1 includes: crushing fresh cassava leaves, mixing the crushed cassava leaves with a proper amount of water, adding an alkaline solution to adjust the pH of the mixed solution to 10.0-11.0, and reacting in a water bath at 55-60 ℃ for 2.0-2.5 h; then taking the supernatant, and adding an acid solution to adjust the pH value of the supernatant to 4.3-4.6; and centrifuging the solution after reaction and collecting precipitate to obtain the total protein of the cassava leaves.
In one or more embodiments, the fresh cassava leaves are ground by: putting fresh cassava leaves into liquid nitrogen for 5-10s, and clamping the frozen cassava leaves into a mortar by using forceps for grinding.
In one or more embodiments, the pretreatment results in a purer authentic protein (92.57% content) with low free amino acid content.
In one or more embodiments, the step S2 includes: and (4) washing the cassava leaf total protein obtained in the step (S1) twice by using pure water, then adding deionized water according to the solid-to-liquid ratio of 1:5, adjusting the pH value to 6-9, and adding protease for enzymolysis.
In one or more embodiments, the protease in step S2 is any one of a neutral protease, an alkaline protease and trypsin, or a mixture of an alkaline protease and trypsin.
In one or more embodiments, the step S2 includes one or more of the following features:
(a) when neutral protease is used, adjusting the pH value of the solution to 6-7, and reacting for 2.0-2.5 h at the temperature of 34-37 ℃;
(b) when alkaline protease is used, adjusting the pH value of the solution to 7-9, and reacting for 2-3h at the temperature of 35-38 ℃;
(c) when trypsin is used, the pH of the solution is adjusted to 7-9, and the reaction is carried out for 2-4h at the temperature of 35-38 ℃.
In one or more embodiments, step S3 is performed by ultrafiltration using an ultrafiltration system, and the enzymatic supernatant is separated by a 3kDa ultrafiltration membrane to obtain a polypeptide liquid.
In one or more embodiments, the microwave device used in the microwave heating step has a power of 500-.
The second aspect of the invention aims to provide a cassava leaf polypeptide obtained by any one of the preparation methods.
The third aspect of the present invention is directed to provide the use of the above-mentioned cassava leaf polypeptide, specifically, the cassava leaf polypeptide is added as a raw material to a beverage, a functional nutritional food or a cosmetic.
Compared with the prior art, the preparation method provided by the invention has the advantages of simple steps and high conversion rate. The cassava leaf polypeptide obtained by the preparation method has strong antioxidant effect, so that the cassava leaf polypeptide can be added into beverages or functional nutritional foods to improve the antioxidant health-care effect; meanwhile, the cassava leaf polypeptide is a small molecular polypeptide with the molecular weight less than 3kDa, is beneficial to skin absorption, and can be added into cosmetics for use.
Drawings
FIG. 1 is a graph showing a comparison of DPPH clearance of cassava leaf polypeptides obtained in examples 1 to 3 with Vc.
FIG. 2 is a comparison of the hydroxyl radical scavenging activity of cassava leaf polypeptides obtained in examples 1-3 with Vc.
FIG. 3 shows the results of the total reducing power of the cassava leaf polypeptides and Vc obtained in examples 1 to 3.
FIG. 4 is an HPLC chromatogram of the derivatized cassava leaf polypeptide obtained in example 1.
Detailed Description
The present invention will be described in detail below. The technical features described below are explained based on typical embodiments and specific examples of the present invention, but the present invention is not limited to these embodiments and specific examples. It should be noted that:
in the present specification, the numerical range represented by "numerical value a to numerical value B" means a range including the end point numerical value A, B.
In the present specification, the numerical ranges indicated by "above" or "below" mean the numerical ranges including the numbers.
In the present specification, the meaning of "may" includes both the meaning of performing a certain process and the meaning of not performing a certain process.
As used herein, the term "optional" or "optional" is used to indicate that certain substances, components, performance steps, application conditions, and the like are used or not used.
In the present specification, the unit names used are all international standard unit names, and the "%" used means weight or mass% content, if not specifically stated.
In the present specification, the term "plurality" means two or more than two unless otherwise specified.
In the present specification, reference to "some particular/preferred embodiments," "other particular/preferred embodiments," "embodiments," and the like, means that a particular element (e.g., feature, structure, property, and/or characteristic) described in connection with the embodiment is included in at least one embodiment described herein, and may or may not be present in other embodiments. In addition, it is to be understood that the described elements may be combined in any suitable manner in the various embodiments.
Example 1
A preparation method of cassava leaf polypeptide comprises the following steps:
s1, putting fresh cassava leaves into liquid nitrogen for 5S, and clamping the frozen cassava leaves into a mortar by using forceps for grinding; mixing the grinded cassava leaves with a proper amount of water, adding a sodium hydroxide solution to adjust the pH of the mixed solution to 10.0, and reacting in a water bath at 55 ℃ for 2 hours; then taking the supernatant, adding a hydrochloric acid solution to adjust the pH value to 4.3; centrifuging the solution after reaction and collecting precipitate to obtain total protein of the cassava leaves;
s2, washing the cassava leaf total protein obtained in the step S1 twice by using pure water, then adding deionized water according to a solid-to-liquid ratio of 1:5, adjusting the pH value to 6, adding neutral protease (100U/mg, Shanghai-sourced leaf Biotech Co., Ltd.) for enzymolysis, reacting at the temperature of 34 ℃ for 2.0h, and then inactivating enzyme at high temperature;
s3, separating the enzymolysis supernate by using an ultrafiltration system through a ultrafiltration membrane with the molecular weight of 3kDa to obtain polypeptide liquid;
s4, performing microwave heating on the obtained polypeptide liquid for 30S, wherein the power of the adopted microwave device is 500W, and obtaining the cassava leaf polypeptide.
Example 2
A preparation method of cassava leaf polypeptide comprises the following steps:
s1, putting fresh cassava leaves into liquid nitrogen for 7S, and clamping the frozen cassava leaves into a mortar by using forceps for grinding; mixing the grinded cassava leaves with a proper amount of water, adding sodium hydroxide solution to adjust the pH of the mixed solution to 10.5, and reacting in a 56 ℃ water bath for 2 hours; then taking the supernatant, adding a hydrochloric acid solution to adjust the pH value to 4.5; centrifuging the solution after reaction and collecting precipitate to obtain total protein of the cassava leaves;
s2, washing the total cassava leaf protein obtained in the step S1 twice by using pure water, adding deionized water according to the solid-to-liquid ratio of 1:5, adjusting the pH value to 7, adding alkaline protease (50U/mg, Shanghai-sourced leaf Biotech Co., Ltd.) for enzymolysis, and reacting at the temperature of 36 ℃ for 2.5 hours;
s3, separating the enzymolysis supernate by using an ultrafiltration system through a ultrafiltration membrane with the molecular weight of 3kDa to obtain polypeptide liquid;
s4, carrying out microwave heating on the obtained polypeptide liquid for 40S, wherein the power of a microwave device is 550W, and obtaining the cassava leaf polypeptide.
Example 3
A preparation method of cassava leaf polypeptide comprises the following steps:
s1, putting fresh cassava leaves into liquid nitrogen for 8S, and clamping the frozen cassava leaves into a mortar by using forceps for grinding; mixing the grinded cassava leaves with a proper amount of water, adding a sodium hydroxide solution to adjust the pH of the mixed solution to 11.0, and reacting in a water bath at 60 ℃ for 2.5 h; then taking the supernatant, adding a hydrochloric acid solution to adjust the pH value to 4.6; centrifuging the solution after reaction and collecting precipitate to obtain total protein of the cassava leaves;
s2, washing the total cassava leaf protein obtained in the step S1 twice by using pure water, adding deionized water according to the solid-to-liquid ratio of 1:5, adjusting the pH to 9, adding trypsin (100U/mg, Shanghai-sourced leaf Biotech limited) for enzymolysis, and reacting for 4 hours at the temperature of 38 ℃;
s3, separating the enzymolysis supernate by using an ultrafiltration system through a ultrafiltration membrane with the molecular weight of 3kDa to obtain polypeptide liquid;
s4, performing microwave heating on the obtained polypeptide liquid for 35S, wherein the power of a microwave device is 600W, and obtaining the cassava leaf polypeptide.
Example 4
A preparation method of cassava leaf polypeptide comprises the following steps:
s1, putting fresh cassava leaves into liquid nitrogen for 9S, and clamping the frozen cassava leaves into a mortar by using forceps for grinding; mixing the ground cassava leaves with a proper amount of water, adding a sodium hydroxide solution to adjust the pH of the mixed solution to 10.5, and reacting in a water bath at 55-60 ℃ for 2 hours; then taking the supernatant, adding a hydrochloric acid solution to adjust the pH value to 4.5; centrifuging the solution after reaction and collecting precipitate to obtain total protein of the cassava leaves;
s2, washing the cassava leaf total protein obtained in the step S1 twice by using pure water, then adding deionized water according to the solid-to-liquid ratio of 1:5, adjusting the pH to 8.5, adding alkaline protease and trypsin, and reacting for 3 hours at the temperature of 38 ℃; the adding ratio of the alkaline protease to the trypsin is 1: 1;
s3, separating the enzymolysis supernate by using an ultrafiltration system through a ultrafiltration membrane with the molecular weight of 3kDa to obtain polypeptide liquid;
s4, performing microwave heating on the obtained polypeptide liquid for 35S, wherein the power of a microwave device is 600W, and obtaining the cassava leaf polypeptide.
Comparative example 1
A method for producing a cassava leaf polypeptide, substantially the same as in example 1, except that step S4 is omitted.
Comparative example 2
A method for preparing cassava leaf polypeptide, which is substantially the same as in example 1, except that the microwave time of step S4 is 10S.
Comparative example 3
A preparation method of cassava leaf polypeptide, which is basically the same as the example 1, except that the microwave time of the step S4 is 1 min.
Comparative example 4
A preparation method of cassava leaf polypeptide, which is basically the same as that in example 1, except that step S4 is omitted, and enzymolysis is performed under microwave conditions in step S2, the microwave conditions are the same as those in example 1.
Comparative example 5
A cassava leaf polypeptide is prepared substantially as in example 1, except that a microwave apparatus with a power of 1000W is used in step S4.
Comparative example 6
The traditional preparation method of the cassava leaf polypeptide comprises the following steps:
taking about 0.3g of cassava leaves, grinding the cassava leaves by using liquid nitrogen, adding PVP (polyvinyl pyrrolidone) which has more pigment and can be 10% of the fresh weight of the cassava leaves, transferring the fully ground sample into a centrifuge tube, adding 4mL of extraction buffer solution, shaking uniformly, extracting for 1h at 4 ℃, and fully dissolving protein (cassava leaf total protein).
The placed sample is fully shaken up, centrifuged at 10000r/min at 4 ℃ for 30min, the precipitate is discarded, and 2.5-3 times of the volume of the supernatant is added into the supernatant for overnight at-20 ℃ to ensure that the protein is fully precipitated. Then, centrifuging at 4 deg.C 10000r/min for 30min, collecting supernatant, precipitating at-20 deg.C, volatilizing acetone completely, and adding sample buffer solution to dissolve precipitate if necessary. The using amount of the buffer solution is 300ul, the precipitate is fully dissolved, then the precipitate is transferred to a 1.5mL centrifuge tube, centrifugation is carried out for 15min at 12000r/min at 4 ℃, and the supernatant is taken to be the extracted cassava leaf polypeptide.
Detection example 1DPPH scavenging Activity
Refer to Xiaguan (enzyme method preparation of mung bean antioxidant peptide and antioxidant activity [ J ] of mung bean antioxidant peptide, food and biotechnological report) determination method, and make slight modification. Respectively taking 0.2mL of samples to be detected with different concentrations (cassava leaf polypeptides prepared in examples 1-3) and an isometric 0.2mmol/L DPPH-absolute ethanol solution, uniformly mixing, carrying out a reaction at normal temperature in a dark place for 30min, and measuring the absorbance at 517nm, wherein the absorbance is marked as A1; measuring the absorbance of a mixed solution of 0.2mL of sample and 0.2mL of absolute ethyl alcohol, and marking as A2; the absorbance of 0.2mL of a 0.2mmol/LDPPH solution and 0.2mL of distilled water was designated as A3. Vc was used as a positive control. For each 3 replicates, DPPH free radical clearance was calculated as follows:
as can be seen from FIG. 1, when the concentration of the polypeptide is higher than 0.35mg/mL, there is no significant difference in DPPH clearance of the three enzymatic hydrolysates; when the concentration of the polypeptide is 1.5mg/mL, the DPPH clearance rate reaches about 90 percent, and is generally consistent with the DPPH clearance rate of Vc.
Detection example 2Hydroxyl radical scavenging Activity
Yuanyan super (sesame polypeptide prepared by mixed fermentation of sesame seed meal and research on in vitro antioxidant activity thereof [ J ]. genomics and applied biology) and Zhao Xutong (anthocyanin extraction and purification in blueberry processing waste and research on antioxidant activity, Jilin university, Master thesis) were referenced and slightly improved. Respectively preparing samples to be detected (cassava leaf polypeptides prepared in examples 1-3) with different concentrations, sequentially adding 0.2mL of polypeptide extracting solution into 0.2mL of 3mmol/L FeSO4 solution, 6mmol/L salicylic acid-ethanol solution and 6mmol/L H2O2, mixing uniformly, and reacting at normal temperature for 30 min. After the reaction is finished, measuring the light absorption value at 517nm, and recording as A1; the absorbance was measured using deionized water instead of the sample and was designated as A0. The hydroxyl radical scavenging activity is calculated by the following formula:
as can be seen from fig. 2, the hydroxyl radical scavenging activity of the polypeptide obtained by neutral protease is significantly higher than that of the polypeptide obtained by alkaline protease and trypsin; when the concentration of the polypeptide obtained by the neutral protease is 1.5mg/mL, the hydroxyl radical scavenging activity reaches 79.32%; when the Vc concentration is lower than 1.5mg/mL, the hydroxyl radical scavenging activity is obviously lower than that of the polypeptide solution. Therefore, the hydroxyl radical scavenging activity of the cassava leaf polypeptide obtained in example 1 is remarkably higher than that of examples 2 and 3, and the hydroxyl radical scavenging activity of the polypeptide is obviously higher than that of Vc under the condition of low concentration.
Detection example 3Determination of Total reducing force
The method refers to Xiaguan (enzyme method preparation of mung bean antioxidant peptide and antioxidant activity [ J ] of mung bean antioxidant peptide, report of food and biotechnology) and Mafei phenanthrene (research on separation, purification, identification and inhibition mechanism of ACE inhibitory peptide of ginkgo kernel, university of fertilizer industry, Master thesis), and is slightly improved. Preparing samples to be detected with different concentrations (cassava leaf polypeptide prepared in examples 1-3), taking 0.2mL of sample solution, sequentially adding 0.2mL of PBS buffer solution and 0.2mL of 1% potassium ferricyanide solution, reacting in a water bath at 50 ℃ for 30min, adding 0.2mL of 10% trichloroacetic acid solution, uniformly mixing, standing for 10min, centrifuging at 3000 r/min for 5min, taking 0.4mL of supernatant, adding 0.4mL of deionized water and 0.2mL of 0.1% FeCl3 solution, uniformly mixing, standing for 10min, and measuring the absorbance at 700nm wavelength.
As shown in FIG. 3, the total reducing power of the polypeptide obtained by the preparation method of example 1 is slightly higher, and the absorbance reaches 0.558 at a polypeptide concentration of 1.5mg/mL, but is lower than that of Vc. In FIG. 3, the total reducing power of Vc at concentrations of 0.75, 1, and 1.5mg/mL is significantly higher than the polypeptides obtained in examples 1-3, and is therefore not indicated.
Detection example 4Determination of purity
The purity of the cassava leaf polypeptide obtained by the preparation method is judged by comparing the HPLC (high performance liquid chromatography) spectra of the amino acid standard substance and the polypeptide after derivatization.
As shown in FIG. 4, a is the HPLC profile of the amino acid standard, and b is the HPLC profile of the derivatized polypeptide obtained by the preparation method of example 1.
Note: the amino acid classes represented by the numbers in FIG. 4 are as follows: 1. aspartic acid 2, glutamic acid 3, serine 4, glycine 5, histidine 6, arginine 7, threonine 8, alanine 9, proline 10, tyrosine 11, valine 12, methionine 13, cystine 14, isoleucine 15, leucine 16, derivative peak 17, phenylalanine 18, lysine.
As can be seen from FIG. 4, the cassava leaf polypeptide obtained by the preparation method of example 1 has very high purity and few free amino acids. By measuring HPLC (high performance liquid chromatography) spectra obtained after derivatization of the cassava leaf polypeptides obtained in other embodiments, the same free amino acids are found to be few, which indicates that the cassava leaf polypeptides obtained by the preparation method have high purity.
Detection example 5Determination of the conversion of the polypeptide
The total protein content of the cassava leaves obtained in examples 1 to 4 and comparative examples 1 to 6 was measured and recorded as P0;
protein contents of the cassava leaf polypeptides obtained in examples 1 to 4 and comparative examples 1 to 6 were measured, respectively, and are designated as P1;
the conversion (%) of the cassava leaf polypeptide was P1/P0 × 100%, and the results are shown in the following table:
as can be seen from the above table, the conversion rate of the cassava leaf polypeptides obtained by the preparation methods of examples 1 to 4 is significantly higher than that of each comparative example. As can be seen from comparison of examples 1 and comparative examples 1 to 5, the conversion rate of the polypeptide can be significantly improved by subjecting the polypeptide liquid obtained by ultrafiltration to microwave heating under appropriate conditions.
Claims (10)
1. The preparation method of the cassava leaf polypeptide is characterized by comprising the following steps:
s1, preprocessing, and extracting total protein of cassava leaves;
s2, carrying out enzymolysis on the cassava leaf total protein by using protease to obtain an enzymolysis liquid;
s3, carrying out ultrafiltration on the enzymolysis liquid, and collecting polypeptide liquid with the molecular weight lower than 3 kDa;
s4, carrying out microwave heating on the obtained polypeptide liquid for 30-40S to obtain the cassava leaf polypeptide.
2. The method for preparing a composite material according to claim 1, wherein the step S1 includes: crushing fresh cassava leaves, mixing the crushed cassava leaves with a proper amount of water, adding an alkaline solution to adjust the pH of the mixed solution to 10.0-11.0, and reacting in a water bath at 55-60 ℃ for 2.0-2.5 h; then taking the supernatant, and adding an acid solution to adjust the pH value of the supernatant to 4.3-4.6; and centrifuging the solution after reaction and collecting precipitate to obtain the total protein of the cassava leaves.
3. The preparation method according to claim 2, wherein the fresh cassava leaves are crushed by the steps of: putting fresh cassava leaves into liquid nitrogen for 5-10s, and clamping the frozen cassava leaves into a mortar by using forceps for grinding.
4. The production method according to claim 2 or 3, wherein the step S2 includes: and (4) washing the cassava leaf total protein obtained in the step (S1) twice by using pure water, then adding deionized water according to the solid-to-liquid ratio of 1:5, adjusting the pH value to 6-9, and adding protease for enzymolysis.
5. The method according to claim 4, wherein the protease in step S2 is any one of neutral protease, alkali protease and trypsin, or a mixture of alkali protease and trypsin.
6. The method according to claim 5, wherein the step S2 includes one or more of the following features:
(a) when neutral protease is used, adjusting the pH value of the solution to 6-7, and reacting for 2-2.5 h at the temperature of 34-37 ℃;
(b) when alkaline protease is used, adjusting the pH value of the solution to 7-9, and reacting for 2-3h at the temperature of 35-38 ℃;
(c) when trypsin is used, the pH of the solution is adjusted to 7-9, and the reaction is carried out for 2-4h at the temperature of 35-38 ℃.
7. The method according to claim 6, wherein the step S3 is performed by ultrafiltration using an ultrafiltration system, and the enzymatic supernatant is separated by an ultrafiltration membrane having a molecular weight of 3kDa to obtain the polypeptide liquid.
8. The preparation method according to any one of claims 1 to 7, wherein the microwave heating step uses a microwave device with power of 500-600W.
9. Cassava leaf polypeptides obtained by the preparation method according to any one of claims 1 to 8.
10. Use of a cassava leaf polypeptide according to claim 9, wherein the cassava leaf polypeptide is added as a raw material to a beverage, a functional nutritional food or a cosmetic.
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| US20140011742A1 (en) * | 2010-12-09 | 2014-01-09 | Mcgill University | Bioactive Peptides and Proteins Containing Bioactive Peptides, their Uses and Processes for Making the Same |
| CN105368906A (en) * | 2015-12-09 | 2016-03-02 | 南宁知本康业生物技术有限公司 | Microwave-assisted method for preparing cassava leaf protein polypeptides |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| US20140011742A1 (en) * | 2010-12-09 | 2014-01-09 | Mcgill University | Bioactive Peptides and Proteins Containing Bioactive Peptides, their Uses and Processes for Making the Same |
| CN105368906A (en) * | 2015-12-09 | 2016-03-02 | 南宁知本康业生物技术有限公司 | Microwave-assisted method for preparing cassava leaf protein polypeptides |
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| MARYAM NIKBAKHT NASRABADI等: "Modification approaches of plant-based proteins to improve their techno-functionality and use in food products", FOOD HYDROCOLLOIDS, pages 5 * |
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