CN107383159B - Chickpea oligopeptide and industrial preparation method and application thereof - Google Patents
Chickpea oligopeptide and industrial preparation method and application thereof Download PDFInfo
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- CN107383159B CN107383159B CN201710658081.8A CN201710658081A CN107383159B CN 107383159 B CN107383159 B CN 107383159B CN 201710658081 A CN201710658081 A CN 201710658081A CN 107383159 B CN107383159 B CN 107383159B
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Images
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
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- 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
- A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
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- 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
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
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- 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
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Abstract
The invention relates to chickpea oligopeptide and an industrial preparation method and application thereof. The yield of the oligopeptide powder is not lower than 7%, the peptide content is more than 80wt%, the molecular weight is evenly distributed below 1500Dalton, and the ash content is not higher than 5%. The method is simple and convenient to operate, high in yield, low in cost and suitable for large-scale production. The chickpea oligopeptide powder has good antioxidant activity and anti-fatigue effect, has the effects of promoting the secretion of PM2.5 particles by intestinal tracts, enhancing the phagocytosis function of macrophages on the PM2.5 particles and improving the cardiac enlargement caused by the PM2.5 particles, and can be used for preparing medicines, foods or health-care products for treating or preventing symptoms caused by the PM2.5 particles.
Description
Technical Field
The invention provides chickpea oligopeptide, an industrial production process and application thereof, belonging to the field of deep processing of food.
Background
Chickpeas (Cicer arietinum L) are herbaceous plants of Papilionaceae, namely peaches beans, chicken beans, heart beans and the like, are one of important vegetables of India and Pakistan, and are also common in Europe and are also common medical materials for Uygur medicine. Uygur can be used for treating bronchitis, mucositis, cholera, constipation, dysentery, dyspepsia, flatulence, venomous snake bite, diabetes, hyposexuality, skin pruritus, hyperlipidemia, and heatstroke. In traditional Chinese medicine, chickpeas can regulate humidity and have the effects of stopping diarrhea, detoxifying, strengthening the body and the like.
The chickpeas contain abundant nutritional ingredients, which greatly exceed other beans in terms of variety and quantity. It contains more than 18 amino acids (containing all 8 amino acids which are necessary for human body but can not be synthesized by human body), various nutrient elements and trace elements, such as: calcium, cobalt, zinc, magnesium, phosphorus, and the like. In particular, each hundred grams of chickpeas contains 350 mg of calcium and 320 mg of phosphorus, which are higher than most beans, the content of iron reaches 47 mg, which is higher than that of other beans by 90%, the content of vitamins C, B1 and B2 reaches 12 mg, and the content of dietary fiber is higher than that of other beans. Chickpeas are reported to be abundant in protein, up to 20%, with globulin and albumin accounting for 42.16% and 39.76% of total protein, respectively. Globulin and albumin are very important nutrients for human body and can play a role in improving immunity. Compared with chickpea protein, the hydrolysate chickpea oligopeptide has the characteristic of high-quality protein like the chickpea protein in amino acid composition, has physicochemical properties such as good solubility and stability which are not possessed by the chickpea protein, and has various physiological functions such as easy absorption and low allergen, blood fat and cholesterol reduction, blood pressure reduction, promotion of mineral substance absorption and fat metabolism, physical ability enhancement of athletes and the like, so the development of the chickpea oligopeptide becomes a research hotspot in the field of food and medicines. Our earlier patent CN 105949290 a discloses a process for preparing chickpea protein and its peptides, wherein the yield of chickpea peptide is about 6%, the peptide content is not less than 80wt%, the molecular weight of more than 85% of peptides is less than 1500Dalton, and the ash content is about 10%. In order to obtain the chickpea oligopeptide with smaller high molecular weight and lower ash content and be applied to industrial production, the invention provides a better preparation process of the chickpea oligopeptide, the molecular weight of the prepared chickpea oligopeptide is distributed below 1500Dalton, the ash content is controlled below 5 percent, and the yield is also improved to a certain extent. Meanwhile, biological activity experiments show that the chickpea oligopeptide powder produced by the process also has better antioxidant activity, and in-vivo biological activity tests show that the chickpea oligopeptide powder has better anti-fatigue effect and can be used for preparing medicaments, foods or health-care products for treating related diseases. In addition, the in vivo activity also shows that the peptide powder has the effects of promoting the secretion of PM2.5 particles by intestinal tracts, enhancing the phagocytic function of macrophages on the PM2.5 particles and improving the cardiac enlargement caused by the PM2.5 particles, and can be used for preparing medicines, foods or health-care products for treating or preventing the symptoms caused by the PM 2.5.
The food contains abundant inorganic components in addition to a large amount of organic substances. These inorganic components maintain the normal physiological functions of the human body and play an important role in constituting human tissues. The inorganic substances left after the food is burned at high temperature are called ash. The ash content is mainly mineral salt or inorganic salt in food, and the measurement of the ash content in the food is one of indexes for evaluating the quality of the food. Ash is an important quality indicator for the food industry. For example, in flour processing, the flour is often rated for total ash content, since wheat bran has an ash content that is about 20 times higher than the endosperm, and thus, the higher the processing accuracy of the flour, the lower the ash content. In the production of pectin, gelatin, and other gum products, the total ash content may be indicative of the jelly properties of these products; the water-soluble ash content indicates the fruit content in fruit products such as jam, jelly and the like to a great extent; while an increase in acid insoluble ash is indicative of contamination and adulteration. This is important to ensure the quality of the food. The control of ash in food and pharmaceutical products has the following important implications:
(1) the total ash content of the food is an important basis for controlling the quality of finished or semi-finished food products. Such as: the total ash content of milk is constant in milk. Generally from 0.68% to 0.74%, with an average value very close to 0.70%, so that it is possible to determine whether the milk is adulterated or not, and if so, the ash content is reduced, by determining the total ash content in the milk. In addition, the concentration ratio can be judged, and if the ash content of the milk is detected to be about 1.4%, the milk is concentrated by one time. For example, the wheat flour is rich in wheat bran ash, the endosperm of the wheat flour is rich in protein, and the ash content of the wheat bran is 20 times higher than that of the endosperm, namely, the flour has high precision, and the ash content is low.
(2) And (4) evaluating whether the food is sanitary and has no pollution. Different foods have different compositions and contents of various ashes due to different raw materials, processing methods and measuring conditions, and the ashes of certain foods are always in a certain range when the conditions are determined. If the ash content exceeds the normal range, it indicates that raw materials or food additives which are not in accordance with the hygienic standards are used in the production of foods or that the foods are contaminated during the processing, storage and transportation. Therefore, measuring ash content can determine the degree of food contamination
(3) And judging whether the food is adulterated.
(4) Reference indicators for nutrition (by measuring various elements) were evaluated.
(5) The processing precision and the food quality of the food can be judged. Inorganic salt is one of six nutritional elements, is an indispensable substance for human life activities, and is an evaluation index for correctly evaluating the nutritional value of certain food. For example, flour is often rated by total ash content, with a floury flour of 0.3-0.5%; the standard powder is 0.6-0.9%. In the production of gums such as pectin and gelatin, ash is an indicator of the jelly performance of these products.
Therefore, in order to obtain the chickpea oligopeptide powder with lower ash content, the ash content of the product prepared by the method can be controlled to be below 5%, and meanwhile, the preparation process is green and environment-friendly and is suitable for large-scale production.
Disclosure of Invention
The invention discloses a chickpea oligopeptide and an industrial preparation process thereof, aiming at providing the industrial preparation process of the chickpea oligopeptide with smaller molecular weight and lower ash content on the premise of ensuring the peptide content, and the process is simpler, more convenient, green and environment-friendly and is suitable for large-scale production. The chickpea oligopeptide powder produced by the process has better antioxidant activity, and can be used for medicines, foods or health-care foods for treating or preventing symptoms caused by excessive free radicals; has antifatigue effect, and can be used in medicine, food or health food for preventing or treating fatigue symptoms; has the effects of promoting the secretion of PM2.5 particles by intestinal tracts, enhancing the phagocytic function of macrophages on the PM2.5 particles and improving the cardiac enlargement caused by the particles, and can be used for preparing medicines, foods or health-care products for treating or preventing the symptoms caused by the PM2.5 particles.
In the preparation process of the chickpea oligopeptide, hydrochloric acid and sodium hydroxide are continuously added in order to reach the reaction condition of biological enzyme in the processes of protein extraction and enzymolysis, so that the content of salt is high, and the ash content is high. Higher ash content affects the peptide content of the product. Because the molecular weight of the salt is small, the former peptide purification method is an ultrafiltration membrane with large molecular weight, and the finally collected permeate of the ultrafiltration membrane is the permeate of the ultrafiltration membrane, so that the peptide, the amino acid and the salt are all in the permeate and the salt cannot be removed.
Ash content of various foods in the prior art is controlled to 8 wt%, such as national standard for soy peptide meal (GBT 22492-. However, the ash content can be controlled below 5wt% by the preparation method of the present application.
In order to achieve the purpose, the invention adopts the technical scheme that:
a chickpea oligopeptide, which is characterized in that: by adopting the detection method of GB/T22492-:
number average molecular weight range: 45 to 1340
Weight average molecular weight range: 47 to 1380;
wherein the ash is less than 5 wt%;
preferably, the peptide content is more than 81.2wt%, and the content of 100% with the molecular weight less than 1500 Dalton;
preferably, the peptide content is more than 85wt%, and the content of 100% with the molecular weight less than 1500 Dalton;
preferably, the peptide content is more than 90wt%, and the content of 100% with the molecular weight less than 1500 Dalton;
preferably, the peptide content is 95wt% or more and the molecular weight is 100% or less than 1500 Dalton.
The invention also provides a preparation method of the chickpea oligopeptide powder; preferably, comprises (1) pretreatment of chickpeas; (2) extracting protein by alkali extraction and acid precipitation; (3) carrying out proteolysis; (4) and (5) separating and purifying.
Preferably, the method comprises the steps of:
(1) pretreatment of raw materials: crushing chickpeas with skins, sieving the chickpeas with a sieve of more than 24 meshes to obtain chickpeas powder, mixing the chickpeas powder with an organic solvent according to the mass ratio of 1: 3-1: 10, stirring at room temperature for 20-60 min, carrying out centrifugal filtration, treating bean dregs again for 1-2 times according to the steps, and finally carrying out centrifugal filtration to obtain the treated bean dregs.
(2) Extracting protein by an alkali extraction and acid precipitation method: mixing the processed bean dregs with water according to a weight ratio of 1: 5-1: 20, adjusting the pH to 8-10, extracting at room temperature for 2-3 times, each time for 1-2 hours, combining alkali extract, carrying out centrifugal filtration, adjusting the pH of filtrate to 3-5, centrifuging, removing supernatant, cleaning precipitate with purified water with the pH of 3-5 for 1-2 times, and centrifuging to obtain chickpea protein precipitate.
(3) And (3) proteolysis: adding purified water with a volume ratio of 1: 5-1: 15 into the chickpea protein precipitate, mixing, uniformly stirring for redissolving, heating the protein redissolution to 40-55 ℃, adding 0.1-1% of biological enzyme by mass of the chickpea powder, stirring for enzymolysis for 4-6 h, adjusting the pH to 2-6, boiling for inactivation for 10-30 min, and performing centrifugal filtration to obtain a filtrate for later use;
(4) separation and purification: and (3) filtering the filtrate obtained in the step (3) by using a microfiltration membrane with the aperture of less than 0.5 mu m, treating the permeate by using a 100-400 Dalton nanofiltration membrane, and concentrating and drying the trapped fluid to obtain the chickpea oligopeptide powder.
Preferably, the organic solvent is selected from one of alcohols, lipids, ethers, alkanes or a mixture thereof, preferably ethanol solution; the ethanol used for preparing the ethanol solution is food grade ethanol, and the volume concentration of the ethanol solution is more than 50%, preferably more than 90%.
Preferably, the alkali extraction and acid precipitation method can be a continuous countercurrent extraction method or a common extraction method.
Preferably, the biological enzyme is selected from one of food-grade neutral protease (the enzyme activity is more than or equal to 30 ten thousand u/g), papain (the enzyme activity is more than or equal to 40 ten thousand u/g), bromelain (the enzyme activity is more than or equal to 30 ten thousand u/g), alkaline protease (the enzyme activity is more than or equal to 20 ten thousand u/g), pepsin (the enzyme activity is more than or equal to 50 ten thousand u/g), pancreatin (the enzyme activity is more than or equal to 3000u/g) or a mixture of the neutral protease and the neutral protease is preferably used.
Preferably, the concentration may be membrane concentration, concentration under reduced pressure or concentration under normal pressure; the drying may be spray drying, vacuum drying, heat drying or freeze drying.
The preparation method of the chickpea oligopeptide powder is characterized by comprising the following steps: the yield of chickpeas is above 7%.
More preferably, the preparation method comprises a step of processing by using a nanofiltration membrane of 100-400 Dalton in the separation and purification step.
The invention also provides a composition which contains the chickpea oligopeptide powder and pharmaceutically or food acceptable auxiliary agents.
The dosage form of the composition is selected from plain tablets, film-coated tablets, sugar-coated tablets, enteric-coated tablets, dispersible tablets, capsules, granules, oral solution or oral suspension.
The chickpea oligopeptide powder and the composition are all used for preparing medicines, foods or health-care products for treating or preventing symptoms caused by excessive free radicals. The chickpea oligopeptide powder is prepared from neutral protease.
The chickpea oligopeptide powder and the composition are used for preparing foods, health-care products or medicines for preventing or relieving fatigue, more preferably fatigue caused by strenuous exercise or mental stress, and more preferably fatigue caused by strenuous exercise. The chickpea oligopeptide powder is prepared from neutral protease.
The chickpea oligopeptide powder and the composition are applied to preparing medicines, foods or health-care products which can promote the secretion of PM2.5 particles by intestinal tracts, enhance the phagocytic function of macrophages on the PM2.5 particles and improve the cardiac enlargement caused by the PM2.5 particles. The chickpea oligopeptide powder is prepared from neutral protease.
Drawings
FIG. 1: the liquid chromatogram of the peptide powder prepared by the method is shown;
FIG. 2: a phenotype diagram of the effect of chickpea oligopeptide powder on promoting the secretion of nano activated carbon (PM 2.5) in zebra fish bodies into intestinal tracts;
FIG. 3: a phenotype diagram of the phagocytic function promoting effect of the chickpea oligopeptide powder on the phagocytic function of the nano activated carbon (PM 2.5) phagocytosed macrophages in the zebra fish body;
FIG. 4: a phenotype diagram of the heart enlargement improvement effect of the chickpea oligopeptide powder on the zebra fish caused by the nano activated carbon (PM 2.5).
Examples
The invention is further illustrated by the following examples. It should be understood that the method described in the examples is only for illustrating the present invention and not for limiting the present invention, and that simple modifications of the preparation method of the present invention based on the concept of the present invention are within the scope of the claimed invention. All the raw materials and solvents used in the examples are commercially available products unless otherwise specified. The amounts of the product of the invention and the positive control drug used in active examples 2 and 3 were both added according to the maximum tolerated dose of the test recipient.
Comparative example:
peptide powder obtained by the preparation method of patent CN 105949290 a: pulverizing semen Ciceris Arietini, and sieving with 24 mesh sieve to obtain semen Ciceris Arietini powder. Mixing 1kg of chickpea powder with 95% ethanol solution according to the mass ratio of 1:3, stirring at room temperature for 30min, after completion, carrying out centrifugal filtration, carrying out again treatment on bean dregs according to the steps, and carrying out centrifugal filtration; mixing bean dregs with purified water with a mass ratio of 1:8, adjusting pH to 9.5, extracting at room temperature for 1h, centrifuging and filtering after extraction is finished, and removing filter residues to obtain filtrate for later use; adjusting the pH of the filtrate to 3, centrifuging and removing supernatant, and cleaning the protein precipitate once by using purified water with the pH of 3; adding purified water with a volume ratio of 1:5 into the cleaned protein precipitate, uniformly stirring for redissolving, heating the protein redissolution to 45 ℃, adding neutral protease (the enzyme activity is 40 ten thousand u/g) accounting for 0.2% of the mass of the chickpea powder, stirring for enzymolysis for 4 hours, boiling for inactivation for 10min, centrifuging, and obtaining supernatant fluid which is protein enzymolysis liquid; filtering the protein enzymolysis liquid by using a microfiltration membrane with the aperture of 0.5 mu m, treating the permeate by using a 5000Dalton ultrafiltration membrane, concentrating and drying the trapped fluid to obtain light yellow chickpea oligopeptide powder (T-2), wherein the yield can reach 6.1%, the peptide content is 80.7%, at least more than 95.41% of the peptide content is distributed below 1500Dalton molecular weight, and the ash content is 10.8 wt%.
Peptide powder obtained by the process of the invention: pulverizing semen Ciceris Arietini, and sieving with 24 mesh sieve to obtain semen Ciceris Arietini powder. Mixing 1kg of chickpea powder with 95% ethanol solution according to the mass ratio of 1:3, stirring at room temperature for 30min, after completion, carrying out centrifugal filtration, carrying out again treatment on bean dregs according to the steps, and carrying out centrifugal filtration; mixing bean dregs with purified water with a mass ratio of 1:8, adjusting pH to 9.5, extracting at room temperature for 1h, centrifuging and filtering after extraction is finished, and removing filter residues to obtain filtrate for later use; adjusting the pH of the filtrate to 3, centrifuging and removing supernatant, and cleaning the protein precipitate once by using purified water with the pH of 3; adding purified water with a volume ratio of 1:5 into the cleaned protein precipitate, uniformly stirring for redissolving, heating the protein redissolution to 45 ℃, adding neutral protease (the enzyme activity is 40 ten thousand u/g) accounting for 0.2% of the mass of the chickpea powder, stirring for enzymolysis for 4h, adjusting the pH to 3, boiling for inactivation for 10min, centrifuging, and obtaining a supernatant which is a protein enzymolysis liquid; filtering the protein enzymolysis liquid by using a microfiltration membrane with the aperture of 0.1 mu m, treating the permeate by using a 100Dalton nanofiltration membrane, concentrating and drying the trapped fluid to obtain light yellow chickpea oligopeptide powder (T-1), wherein the yield can reach 7.3%, and the peptide content is measured to be 81.2wt%, and the peptide molecular weight is less than 1500 Dalton. Therefore, on the premise of not influencing the peptide content, the yield is improved by 1%, the molecular weight is smaller, the molecular weight is less than 1500Dalton below which is less than 1500Dalton and accounts for 100%, and the ash content is 3.8 wt%.
Biological activity example 1 (antioxidant activity):
1 DPPH free radical scavenging experiment:
1.1 preparation of ethanol solution of DPPH: accurately weighing DPPH 4mg, placing in a 100mL brown volumetric flask, adding 50mL ethanol, performing ultrasonic treatment for 30s, fixing the volume to the scale with the ethanol, and shaking up for later use. It should be used in situ.
1.2 preparation of test solution: accurately weighing appropriate amount of semen Ciceris Arietini oligopeptide powder, adding ethanol for dissolving, diluting to desired volume, and diluting to desired concentration.
1.3, operation steps: accurately sucking 2mL of a test solution and 2mL of a DPPH solution, and uniformly mixing; accurately sucking 2mL of test solution and 2mL of ethanol, and uniformly mixing; accurately absorbing 2mL of DPPH solution and 2mL of ethanol, uniformly mixing, standing at room temperature for 30min, measuring absorbance at the wavelength of 515nm, and calculating the free radical clearance according to the following calculation formula:
IR％＝[1-(Ai-Aj)/A0]*100％；
wherein Ai represents the absorbance of the solution after the solution to be detected and DPPH are mixed;
aj represents the absorbance of the solution after the solution to be detected and the solvent are mixed;
a0 represents the absorbance of a solution after mixing DPPH with a solvent.
2 ABTS+Radical scavenging experiments:
2.1 preparation of PBS buffer: weighing 8g of sodium chloride, 0.2g of potassium chloride, 0.24g of potassium dihydrogen phosphate and 3.62g of disodium hydrogen phosphate dodecahydrate, putting the materials into a 1000mL beaker, adding 800mL of distilled water, stirring to dissolve the materials, adjusting the pH value to 7.4 by using hydrochloric acid or sodium hydroxide, transferring the materials into a 1000mL volumetric flask, adding distilled water to dilute the materials to a scale, and shaking the materials uniformly for later use.
2.2 ABTS+Preparation of a storage solution: ABTS is weighed to precision+Placing the mixture into a 20mL brown volumetric flask, adding 15mL distilled water, carrying out ultrasonic treatment for 5min, fixing the volume to the scale with the distilled water, and shaking up. Accurately weighing about 76mg of potassium persulfate, placing the potassium persulfate in a 2mL brown volumetric flask, adding 1mL of distilled water, performing ultrasonic dissolution, fixing the volume to the scale with the distilled water, and shaking up. Add 352. mu.L of potassium persulfate solution to the ABTS solution with precision, shake up, and stand overnight.
2.3 ABTS+Preparing a working solution: accurately pipette 1mL of the storage solution, add about 65mL of PBS buffer, and shake well.
2.4 preparation of test solution: accurately weighing a proper amount of chickpea oligopeptide, adding PBS buffer solution to dissolve, fixing the volume, and diluting to the required concentration.
2.5, operation steps: accurately sucking 0.5mL of test solution and 5mL of ABTS working solution, and uniformly mixing; accurately sucking 0.5mL of test solution and 5mL of PBS buffer solution, and uniformly mixing; accurately pipette 5mL of ABTS working solution and 0.5mL of PBS buffer, mix well, immediately measure absorbance at 734nm, and calculate the radical clearance according to the following formula:
IR％＝[1-(Ai-Aj)/A0]*100％；
wherein Ai represents the absorbance of the solution after the solution to be tested and the ABTS are mixed;
aj represents the absorbance of the solution after the solution to be detected and the solvent are mixed;
a0 represents the absorbance of the solution after mixing ABTS and solvent.
3 SRSA superoxide anion radical scavenging experiment:
3.1 preparation of NBT solution: weighing 24.5mg of nitrotetrazolium chloride (NBT) precisely, placing the mixture in a 100mL brown volumetric flask, adding 50mL of distilled water, carrying out ultrasonic treatment for 30s, fixing the volume to the scale with the distilled water, and shaking up for later use.
3.2 preparation of NADH solution: accurately weighing 33.2mg of nicotinamide adenine dinucleotide reduced coenzyme I (NADH), placing the nicotinamide adenine dinucleotide reduced coenzyme I (NADH) into a 100mL brown volumetric flask, adding 50mL of distilled water, carrying out ultrasonic treatment for 30s, fixing the volume to the scale with the distilled water, and shaking up for later use.
3.3 preparation of PMS solution: 4.59mg of Phenazine Methosulfate (PMS) is precisely weighed, placed in a 250mL brown volumetric flask, added with 150mL of distilled water, subjected to ultrasonic treatment for 30s, and fixed to the scale with the distilled water, and shaken up for later use.
3.4 preparation of Tris-HCl buffer solution: precisely weighing 3.025g of Tris (hydroxymethyl) aminomethane (Tris) and placing the Tris (hydroxymethyl) aminomethane (Tris) in a 500mL beaker, adding 200mL of distilled water, stirring to dissolve the Tris (hydroxymethyl) aminomethane, adjusting the pH to 8.0 with 1M HCl, transferring the Tris (hydroxymethyl) aminomethane to a 250mL volumetric flask, fixing the volume to the scale with distilled water, and shaking up for later use. When in use, 16mL of the solution is put into a 100mL volumetric flask and is diluted to the scale by adding distilled water.
3.3 preparation of test solution: accurately weighing a proper amount of chickpea oligopeptide, adding Tris-HCl buffer solution for dissolving, fixing the volume, and diluting to the required concentration.
3.4 light absorption value detection and free radical clearance calculation: accurately absorbing 1mL of NADH solution, 1mL of NBT solution and 3mL of test solution, adding 3mL of Tris-HCl buffer solution as a control, respectively uniformly mixing, adding 1mL of PMS solution respectively, uniformly mixing, standing at room temperature for 5min, measuring absorbance at 558nm, and calculating the free radical clearance by the following formula:
IR％(SRSA)＝(1-Ai/A0)*100％
wherein Ai represents the absorbance of the solution after the solution to be detected and the detection reagent are mixed;
a0 represents the absorbance of the solution after mixing the blank solution and the detection reagent.
The chick pea oligopeptide products (lots T-1 and T-2) of the comparative examples were prepared separately for DPPH, SRSA and ABTS + free radical scavenging experiments and their EC were determined50Values, results are shown in table 1:
TABLE 1 chickpea oligopeptide powder antioxidant Activity
As can be seen from Table 1, the chickpea oligopeptide powders prepared by the two methods have strong scavenging effect on DPPH and ABTS free radicals, and have weak scavenging effect on superoxide anions (SRSA). The chickpea oligopeptide (T-1) prepared by the method disclosed by the patent has slightly good effect of eliminating three free radicals, and the reason is presumed to be smaller peptide molecular weight. Therefore, the chickpea oligopeptide powder prepared by the method can be also used for preparing medicines, foods or health-care foods for treating or preventing symptoms caused by excessive free radicals.
Biological activity example 2 (anti-fatigue efficacy):
1 improving effect of chickpea oligopeptide on movement ability of zebra fish
4dpf of wild type AB strain zebra fish is randomly selected to be placed in a six-hole plate, 30 tails of each hole (namely each test sample group) are respectively dissolved with water and are given with chickpea oligopeptides, the positive control medicament of Chinese traumatic injury pill has the concentration of 1.0mg/mL, a normal control group and a model control group are simultaneously arranged, and the volume of each hole is 3 mL. After the test article is pretreated for a period of time, the other experimental groups except the normal control group are simultaneously dissolved with water and are given sodium sulfite to induce the zebra fish fatigue model. After the zebra fish is treated by the test sample and sodium sulfite for a period of time, 10 zebra fish are randomly selected from each experimental group, the total movement distance (S) of the zebra fish is determined by using behavior analysis, and the movement improvement effect of the test sample on the fatigue zebra fish induced by the sodium sulfite is quantitatively evaluated.
2 Effect of chickpea oligopeptide on lactic acid metabolism in zebra fish
Randomly selecting 4dpf wild type AB strain zebra fish in a six-hole plate, dissolving 30 tail parts of each hole (namely each test sample group) in water respectively, and giving chickpea oligopeptide, wherein the concentration of a positive control medicament, namely the Chinese traumatic injury pill is 1.0mg/mL, a normal control group and a model control group are simultaneously arranged, and the volume of each hole is 3 mL; each experimental group was set up in 3 replicates. After the test article is pretreated for a period of time, the other experimental groups except the normal control group are simultaneously dissolved with water and are given sodium sulfite to induce the zebra fish fatigue model. After the zebra fish is treated by the test article and sodium sulfite for a period of time, the zebra fish in 3 parallel experimental groups are gathered together (total 90 pieces) in each experimental group, the content of lactic acid in the zebra fish is indirectly measured by utilizing a NanoDrop2000 ultramicro spectrophotometer, and the influence of the chickpea oligopeptide on the content of lactic acid in fatigue zebra fish induced by sodium sulfite under the concentration of 2000 mu g/mL is respectively and quantitatively evaluated.
TABLE 2 improving effect of chick pea oligopeptide on the locomotor ability of zebra fish
TABLE 3 Effect of chick pea oligopeptide on lactic acid content in Zebra Fish
As can be seen from tables 2 and 3, the chickpea oligopeptide powder prepared by the invention can obviously improve the athletic ability of zebra fish and improve the metabolism of lactic acid in vivo. Therefore, the chickpea oligosaccharide powder has obvious anti-fatigue effect and can be used for foods, health-care products or medicines for preventing or relieving fatigue.
Biological activity example 3 (anti-PM 2.5 efficacy):
1 evaluation of the effect of chickpea oligopeptide powder on promoting the secretion of zebra fish nano activated carbon (PM 2.5) into the intestinal tract
Experimental animals: melanin allele mutant translucent Albino strain zebrafish, in a natural pairwise mating breeding mode. The age was 2 days after fertilization, 150 in total, and 30 in each experimental group.
Establishing an experimental model: 62.5mg/mL nano activated carbon (PM 2.5) is used as nano particles and is injected into a yolk sac of 2dpf zebra fish (equivalent to human intramuscular injection), and each zebra fish is injected with 10nL, namely a zebra fish PM2.5 secretion model is established at a dosage of 625 ng/tail.
The experimental steps are as follows: randomly selecting 150 black pigment allele mutant type semitransparent Albino strain zebra fish 2 days (2dpf) after fertilization into a six-well plate, wherein each well (experiment group))30 zebra fish are treated, and nanometer activated carbon is given through intramuscular injection to establish a zebra fish nanometer activated carbon secretion and intestinal function evaluation model. The chick pea oligopeptide (T-1) was dissolved in water to a concentration of 2000. mu.g/mL, while a normal control group (water-treated zebrafish for fish farming) and a model control group were set to have a volume of 3mL per well (experimental group). And (3) changing the liquid of the test sample every day, processing for 5d, counting the number (N) of zebra fish secreted into the intestinal tract by the nano activated carbon in vivo, and evaluating the influence of the test sample on the secretion of the nano activated carbon into the intestinal tract according to the statistical significance of the secretion incidence rate of the nano activated carbon. The statistical treatment result is expressed by mean + -SE, and the nano-active carbon secretion incidence calculation formula is as follows: secretion incidence (%) - (N)The nanometer active carbon is secreted into intestinal tract/NTotal number of) X 100%. The results of the experiment are shown in table 4.
TABLE 4 promoting effect of chickpea oligopeptide powder on intestinal tract secretion of zebra fish
As shown in Table 4, the tail number of the model control group zebra fish nanometer activated carbon secretion is 4/30, and the incidence rate of the nanometer activated carbon secretion is 13.3%. When the concentration of the chickpea oligopeptide is 2000 mug/mL, the tail number of the zebra fish nano activated carbon secretion is 16/30, and the incidence rate of the nano activated carbon secretion is 53.3%, which shows that the chickpea oligopeptide has the function of obviously promoting the zebra fish nano activated carbon secretion to enter the intestinal tract.
2 evaluation of the promoting action of chickpea oligopeptide powder on the phagocytic function of macrophages phagocytosing nano activated carbon (PM 2.5)
Experimental animals: melanin allele mutant translucent Albino strain zebrafish, in a natural pairwise mating breeding mode. The age was 2 days after fertilization, 180 total, 30 in each experimental group.
Establishing an experimental model: 62.5mg/mL nano activated carbon (PM 2.5) is used as nano particles and is injected into the blood circulation of 2dpf zebra fish (equivalent to human intravenous injection), 10nL of nano activated carbon is injected into each zebra fish, and the zebra fish PM2.5 phagocytosis model is established at 625 ng/tail dose.
The experimental steps are as follows: and randomly selecting 180 black pigment allele mutant type semitransparent Albino strain zebra fishes 2 days (2dpf) after fertilization in a six-hole plate, treating 30 zebra fishes in each hole (experimental group), and giving nano activated carbon for intravenous injection to establish a zebra fish nano activated carbon phagocytosis model. The concentration of the chick pea oligopeptide powder (T-1) was 2000. mu.g/mL when dissolved in water, and a normal control group (water-treated zebrafish for fish farming) and a model control group were set at the same time, and the volume per well (experimental group) was 3 mL. Changing the liquid of the test sample every day, adding neutral red solution to perform vital body staining on the zebra fish for 16h after 2d of treatment, counting the number (N) of macrophages engulfming the nano activated carbon under a dissecting microscope after the staining is finished, and evaluating the influence of the test sample on the phagocytosis of the macrophages according to the statistical significance of the number of the macrophages engulfming the nano activated carbon. Statistical treatment results are expressed as mean ± SE, and macrophage phagocytosis promotion was calculated by the formula: macrophage phagocytosis promoting effect (%) ═ NTest article-NModel control group)/NModel control groupX 100%. The results are shown in Table 5.
TABLE 5 promoting effect of chickpea oligopeptide powder on phagocytic function of zebra fish macrophages
As can be seen from Table 5, the number of macrophages phagocytosing the nano activated carbon by the model control group was 11.1, while the number of macrophages phagocytosing the nano activated carbon was 17.9 at 2000. mu.g/mL of the chickpea oligopeptide, and the macrophage phagocytosis promotion effects were 61%, respectively, indicating that the chickpea oligopeptide has an obvious promotion effect on the phagocytosis function of the zebra fish macrophages.
3 evaluation of the improving Effect of chickpea oligopeptide powder on PM 2.5-induced cardiac dilatation
Experimental animals: wild type AB strain zebrafish, in a natural mated mating breeding mode. The age was 2 days after fertilization, 180 total, 30 in each experimental group.
Establishing an experimental model: 2dpf wild type AB strain zebrafish was treated with PM2.5 for 24h to establish a PM2.5 induced cardiovascular toxicity model.
The experimental steps are as follows: wild type AB strain zebra fish 2 days (2dpf) after 180-tail fertilization are randomly selected to be placed in a six-hole plate, 30 zebra fish are treated in each hole (experimental group), and PM2.5 is given in water to induce the zebra fish cardiovascular toxicity evaluation model. The chick pea oligopeptide powder (T-1) was separately administered in water at a concentration of 100. mu.g/mL, while a normal control group (water-treated zebrafish for fish farming) and a model control group were set to have a volume of 3mL per well (experimental group). After being treated with PM2.5 for 24h respectively, 10 zebra fish are randomly selected for each experimental group, photographed under a dissecting microscope and collected, and subjected to image analysis by NIS-Elements D3.10 advanced image processing software to count the heart area (A) of the zebra fish. The statistical treatment results are expressed as mean ± SE, and the test article shows improvement in cardiac enlargement of PM2.5 (%) - (a)Model set-ATest article group)/(AModel set-ANormal control group) X 100%. The results are shown in Table 6.
TABLE 6 amelioration of cardiac dilation induced by chick pea oligopeptide powder on PM2.5
As can be seen from Table 6, the comparison of the cardiac area (13105 pixels) of the zebra fish in the model control group with the normal control group (10590 pixels) shows that the model is successfully established; when the concentration of the chickpea oligopeptide is 100 mug/mL, the heart area of the zebra fish is 11967 pixels, and the heart enlargement improvement effect is 45%, so that the chickpea oligopeptide has a remarkable improvement effect on the heart enlargement caused by PM 2.5.
Claims (7)
1. Application of semen Ciceris Arietini oligopeptide powder in preparing medicine, food or health product for promoting secretion of PM2.5 particulate matter in intestinal tract and improving cardiac enlargement caused by PM2.5 particulate matter; the chickpea oligopeptide is characterized in that: by adopting the detection method of GB/T22492-2008 appendix A and appendix B, the peptide content is measured to be more than 80wt%, the molecular weight is less than 1500Dalton accounting for 100%, and the molecular weight distribution is as follows:
number average molecular weight range: 45 to 1340
Weight average molecular weight range: 47 to 1380;
wherein the ash content is less than 5 wt%.
2. Use according to claim 1, characterized in that: the peptide content is more than 81.2wt%, and the molecular weight is less than 1500Dalton and accounts for 100%.
3. Use according to claim 1, characterized in that: the peptide content is more than 85wt%, and the molecular weight is less than 1500Dalton and accounts for 100%.
4. Use according to claim 1, characterized in that: the peptide content is more than 90wt%, and the molecular weight is less than 1500Dalton and accounts for 100%.
5. Use according to claim 1, characterized in that: the peptide content is more than 95wt%, and the molecular weight is less than 1500Dalton and accounts for 100%.
6. Use according to claim 1, characterized in that: the industrial preparation method of the chickpea oligopeptide comprises the following steps: and (3) treating by using a 100-400 Dalton nanofiltration membrane in the separation and purification step.
7. Use according to claim 1, characterized in that: the industrial preparation method of the chickpea oligopeptide comprises the following steps:
(1) pretreatment of raw materials: crushing chickpeas with skins, sieving the chickpeas with a sieve of more than 24 meshes to obtain chickpeas powder, mixing the chickpeas powder with an organic solvent according to the mass ratio of 1: 3-1: 10, stirring at room temperature for 20-60 min, carrying out centrifugal filtration, treating bean dregs again for 1-2 times according to the steps, and finally carrying out centrifugal filtration to obtain treated bean dregs;
(2) extracting protein by an alkali extraction and acid precipitation method: mixing the processed bean dregs with water according to a weight ratio of 1: 5-1: 20, adjusting the pH to 8-10, extracting at room temperature for 2-3 times, each time for 1-2 hours, combining alkali extract, carrying out centrifugal filtration, adjusting the pH of filtrate to 3-5, centrifuging, removing supernatant, cleaning precipitate with purified water with the pH of 3-5 for 1-2 times, and centrifuging to obtain a chickpea protein precipitate;
(3) and (3) proteolysis: adding purified water with the volume ratio of 1: 5-1: 15 into the chickpea protein precipitate, uniformly stirring and redissolving, and heating the protein redissolution to 40-55%oAdding biological enzyme accounting for 0.1-1% of the mass of the chickpea powder, stirring for enzymolysis for 4-6 hours, adjusting the pH to 2-6, boiling for inactivation for 10-30 min, and performing centrifugal filtration to obtain a filtrate for later use;
(4) separation and purification: filtering the filtrate obtained in the step (3) by using a microfiltration membrane with the aperture of less than 0.5 mu m, treating the permeate by using a 100-400 Dalton nanofiltration membrane, and concentrating and drying the trapped liquid to obtain chickpea oligopeptide powder;
the organic solvent is selected from one of alcohols, lipids, ethers and alkanes or the mixture thereof; the alkali extraction and acid precipitation method is a continuous countercurrent extraction method or a common extraction method;
the biological enzyme is selected from one or a mixture of food-grade neutral protease-enzyme activity of more than or equal to 30 ten thousand u/g, papain-enzyme activity of more than or equal to 40 ten thousand u/g, bromelain-enzyme activity of more than or equal to 30 ten thousand u/g, alkaline protease-enzyme activity of more than or equal to 20 ten thousand u/g, pepsin-enzyme activity of more than or equal to 50 ten thousand u/g and pancreatin-enzyme activity of more than or equal to 3000u/g, and the concentration is membrane concentration, reduced pressure concentration or normal pressure concentration; the drying is spray drying, vacuum drying, heating drying or freeze drying.
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| CN111019989B (en) * | 2018-10-09 | 2022-08-05 | 杏辉天力（杭州）药业有限公司 | Pea oligopeptide powder and preparation method thereof |
| CN112220776B (en) * | 2020-11-18 | 2023-05-05 | 成都医学院 | Chickpea saponin microcapsule and preparation method and application thereof |
| CN112914006B (en) * | 2021-03-09 | 2022-01-25 | 天津渤化讯创科技有限公司 | Hydroxyproline and chickpea composite protein peptide solid beverage and production method thereof |
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