CN106755227B - Method for preparing active peptide metal chelate by laver enzymolysis - Google Patents

Method for preparing active peptide metal chelate by laver enzymolysis Download PDF

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CN106755227B
CN106755227B CN201610980350.8A CN201610980350A CN106755227B CN 106755227 B CN106755227 B CN 106755227B CN 201610980350 A CN201610980350 A CN 201610980350A CN 106755227 B CN106755227 B CN 106755227B
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laver
active peptide
enzymolysis
metal chelate
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CN106755227A (en
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田亚平
胡春芹
龙婧
周楠迪
杜琴
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Jiangnan University
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    • C12P21/00—Preparation of peptides or proteins
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Abstract

The invention relates to a method for preparing active peptide metal chelate by laver enzymolysis, which comprises the following steps: performing enzymolysis reaction on the crushed laver and protease in a buffer solution, and centrifuging and taking supernatant after the enzymolysis is finished; filtering the supernatant, concentrating and drying the filtrate to obtain solid polypeptide powder; and dissolving the solid polypeptide powder in a metal salt aqueous solution to perform a chelation reaction to obtain the laver enzymatic hydrolysis active peptide metal chelate. The invention also discloses application of the laver enzymolysis active peptide metal chelate in preparation of an alpha-glucosidase inhibitor. The invention discloses a novel natural raw material enzymolysis active peptide, which not only has the inhibiting activity of target enzyme, but also can chelate trace metal elements, and the prepared active peptide metal chelate can be quickly absorbed by a human body, thereby playing the roles of supplementing iron and zinc and treating diabetes.

Description

Method for preparing active peptide metal chelate by laver enzymolysis
Technical Field
The invention relates to the technical field of marine active substance biological product production, in particular to a method for preparing active peptide metal chelate by laver enzymolysis.
Background
Diabetes is a hyperglycemia metabolic disease caused by multifactorial action, and the pathogenesis of the diabetes mainly comprises insulin resistance, oxidative stress action, beta cell function damage and cytokine inflammation. At present, the action mechanism for treating diabetes mainly improves the secretion and resistance of insulin and maintains the stable content of islet beta cells. In addition, the use of various enzyme inhibitors in the glycolysis process is also a treatment for diabetes. The condition for preparing the natural alpha-glucosidase inhibitor by the enzymolysis method is controllable, the reaction condition is mild, and the product has stronger inhibitory activity and stronger safety, so that the natural alpha-glucosidase inhibitor is widely concerned by people.
The metal elements such as zinc, iron and the like are one of trace elements necessary for human bodies and are very important for the human bodies. Zinc has a variety of biological functions including participation in glucose and lipid metabolism, cell proliferation, the immune nervous system, and insulin synthesis. Iron is present in all cells of the human body, and is involved in the composition of proteins, an important component constituting the mitochondrial respiratory chain, and a component of many enzymes. The utilization rate of metal elements such as iron, zinc and the like in food is very low, so that a safe and effective nutritional supplement product is found, and the nutritional supplement has important significance for human health.
The polypeptide-metal chelate is used as an organic metal compound, is closer to the action form of metal elements in a body, and can achieve better nutrition supplement effect. And the polypeptide-metal chelate can be transported and absorbed in a polypeptide form, so that competition with amino acid is avoided, the utilization rate of metal elements is improved, and more physiological effects are exerted.
Disclosure of Invention
In order to solve the technical problems, the invention aims to provide a method for preparing active peptide metal chelate by laver enzymolysis, and the invention discloses a novel natural raw material enzymolysis active peptide which not only has the inhibitory activity of target enzyme, but also can chelate trace metal elements, and the prepared active peptide metal chelate can be quickly absorbed by a human body, thereby playing the roles of supplementing iron and zinc and treating diabetes.
The invention relates to a method for preparing active peptide metal chelate by laver enzymolysis, which comprises the following steps:
(1) performing enzymolysis reaction on the crushed laver and protease in a buffer solution, and centrifuging and taking supernatant after the enzymolysis is finished;
(2) filtering the supernatant obtained in the step (1), concentrating and drying the filtrate to obtain solid polypeptide powder;
(3) and (3) dissolving the solid polypeptide powder obtained in the step (2) in a metal salt water solution to perform a chelation reaction to obtain the laver enzymatic hydrolysis active peptide metal chelate.
Further, in step (1), the protease includes alkaline protease, neutral protease and aminopeptidase.
Further, the alkaline protease is a domestic commercial enzyme Bacillus licheniformis alkaline protease. The neutral protease is domestic commercial enzyme subtilisin. The aminopeptidase is a Bacillus subtilis leucine aminopeptidase disclosed in patent CN104293749A by the inventor.
Further, in the step (1), the content of the alkaline protease is 7X 104-9×104U.g-1Thallus Porphyrae with neutral protease content of 7 × 104-9×104U.g-1Thallus Porphyrae with aminopeptidase content of 25-30U.g-1Laver.
Further, in the step (1), the temperature of the enzymolysis reaction is 45-55 ℃, and the enzymolysis time is 5.5-6.5 h.
Further, in step (1), the pH of the buffer solution is 8.0 to 9.0, at which the product prepared has the highest inhibition rate against α -glucosidase.
Further, in the step (1), the concentration of the buffer solution is 20 to 200 mmol/L.
Further, in the step (1), the buffer solution is phosphate buffer or Tris-HCl buffer.
Further, in the step (1), the mass-to-volume ratio of the laver to the buffer solution is 1:30-1:35 g/ml.
Further, in the step (1), the laver is porphyra yezoensis or porphyra haitanensis.
Further, in the step (1), the laver is dried at 40-60 ℃ and then pulverized, and is sieved with a 40-80 mesh sieve, so as to obtain the pulverized laver.
Further, in the step (2), an ultrafiltration membrane with the molecular weight cutoff of 10kDa-30kDa and a nanofiltration membrane with the molecular weight cutoff of 500Da-1kDa are sequentially used for filtering, so that the active peptide with higher purity can be obtained, and the active peptide has good alpha-glucosidase inhibition.
Further, in the step (2), the supernatant is diluted 1.4 to 1.8 times and then filtered.
Further, in the step (2), the concentration of the concentrate is 1mg/ml and 0.5mg/ml of alpha-glucosidase (2X 10)4U.g-1) The inhibition ratio of (2) was 68%.
Further, in the step (2), drying is performed by air spray drying or freeze drying.
Further, in the step (2), the yield of the solid polypeptide powder is 45 to 55%.
Further, in the step (2), the solid polypeptide powder is a bifunctional active peptide which has both alpha-glucosidase inhibitory activity and a function of chelating metal elements.
Further, in the step (3), the metal salt is zinc chloride, zinc nitrate, ferrous chloride or calcium chloride.
Further, in the step (3), the pH value of the chelation reaction is 4.0-5.0, the temperature is 35-40 ℃, and the reaction time is 1.5-2 h.
Further, in the step (3), the mass ratio of the solid polypeptide powder to the metal salt is 6:1-24: 1.
Further, in the step (3), the concentration of the solid polypeptide powder is 2-6mg-1。
Further, in step (3), in order to avoid causing an excessive replenishment of trace elements, the concentration of the aqueous metal salt solution is preferably about 0.5 mmol/L.
Further, in the step (3), the chelating degree of the laver enzymolysis active peptide metal chelate is 25-30%, and the inhibition rate of 0.5mg/ml alpha-glucosidase reaches 79-83% when the concentration of the polypeptide (in the chelate) is controlled to be 1 mg/ml.
The invention also provides application of the laver enzymolysis active peptide metal chelate in preparation of an alpha-glucosidase inhibitor, and the alpha-glucosidase inhibitor can be applied to the fields of food, medicines and health care products.
The laver is subjected to enzymolysis under specific conditions, and after fractional extraction such as centrifugation and membrane filtration, active peptide is prepared, then the active peptide and some specific metal ions are subjected to chelation reaction, the polypeptide chain conformation of the active peptide is changed to a certain extent, the metal ions comprise certain metal elements which have certain inhibitory action on alpha-glucosidase, such as zinc, or metal ions which have no inhibitory action on the alpha-glucosidase, and the inhibitory action of a laver chelate on the alpha-glucosidase is enhanced to a certain extent after the polypeptide chain conformation is changed, so that the inhibition rate of the laver enzymolysis active peptide metal chelate prepared by the invention on the alpha-glucosidase is improved.
By the scheme, the invention at least has the following advantages:
the method utilizes the modern biotechnology to carry out combined controllable enzymolysis on the laver protein to obtain the enzymatic hydrolysate, and has simple chelation process with metal salt and safe product; three kinds of protease are used during enzymolysis, and solid polypeptide powder with glycosidase inhibitory activity is prepared by optimizing enzymolysis conditions, wherein the yield is 45-55%. After the prepared polypeptide is chelated with metal ions, the conformation of the polypeptide is changed, so that the glycosidase inhibition activity of the laver enzymolysis active peptide metal chelate is improved; after chelation with metal, the glycosidase inhibition activity is improved by more than 15 percent compared with that of unchelated polypeptide liquid, and the obtained laver enzymolysis active peptide metal chelate has the health care and treatment functions of medicine and food, and has the promotion and promotion functions on the health development of future medicine and food.
Drawings
FIG. 1 is a flow chart of the method for preparing active peptide metal chelate by enzymolysis of laver;
FIG. 2 is a graph of Zn at various concentrations as a function of alpha-glucosidase inhibition;
FIG. 3 is a graph showing the results of the stability of the time and quality of the laver enzymolysis active peptide metal chelate compound to pepsin in the gastric digestion stage;
FIG. 4 is a graph showing the results of the stability of the time and quality of the laver enzymolysis active peptide metal chelate compound of the present invention to trypsin in the duodenum digestion stage.
Detailed Description
The following detailed description of embodiments of the present invention is provided in connection with the accompanying drawings and examples. The following examples are intended to illustrate the invention but are not intended to limit the scope of the invention.
(1) The method for measuring the alpha-glucosidase inhibition rate comprises the following steps:
by PNPG (4-nitrophenyl-D-glucopyranoside) method, one sample to be tested and one 0.5mg/mL sample are taken-1Mixing alpha-glucosidase uniformly, keeping temperature in water bath at 37 ℃ for 10min, adding a portion of 10 mmol.L-1PNPG, reacting for 1h, adding a 1mol L portion-1Na2CO3The reaction was stopped and the absorbance ai was measured at 405 nm. Taking a sample to be measured and 0.5mg/mL-1Mixing alpha-glucosidase uniformly, keeping the temperature in water bath at 37 ℃ for 10min, adding a part of metal salt solution to react for 1h,then adding a portion of 1 mol.L-1Na2CO3The reaction was stopped and the absorbance aj was measured at 405 nm. Adding a portion of metal salt solution into a centrifuge tube, and then adding a portion of 1 mol. L-1Na2CO3Measuring the absorbance A at 405nm0The inhibition rate of the sample on the activity of alpha-glucosidase was calculated by the following formula:
inhibition rate [1- (Ai-Aj)/A0]×100％
(2) The chelation rate was determined as follows:
the total amount of metals before and after chelation of a sample to be detected is respectively A1 and A2 by adopting a flame atomic absorption spectrophotometer, and the calculation formula of the chelation degree is as follows: the chelating degree is A2/A1.
Example 1 enzymatic hydrolysis and preparation of Porphyra tenera alpha-glucosidase inhibitory active peptides
Taking Porphyra yezoensis as raw material, drying, pulverizing, sieving, adding 40 mesh laver protein dry powder into 20mmol/L NaHCO with pH of 8.53-NaH2CO3In the buffer solution, the ratio of the mass of the dried laver protein powder to the volume of the buffer solution is 1:33 g/mL. Further adding alkaline protease E/S ═ 8X 104U/g, neutral protease 8X 104U/g dry substrate, 28U/g aminopeptidase, at 50 ℃ for 6 h. Alkaline protease is purchased from Pompe, neutral protease is purchased from Sokkehn, and its type is SUKAPro NE, and aminopeptidase is prepared by independent research and development of the inventor, and its preparation method is disclosed in patent CN 104293749A. Inactivating enzyme in boiling water bath, centrifuging, and collecting supernatant. Diluting the supernatant by 1.6 times, passing through 10kDa ultrafiltration membrane and 1kDa nanofiltration membrane respectively, collecting the permeate, concentrating at 50 deg.C by rotary evaporator, vacuum freeze-drying, and collecting lyophilized powder to obtain the active peptide for inhibiting laver alpha-glucosidase.
1mg/ml of freeze-dried powder aqueous solution is prepared, and the alpha-glucosidase inhibition rate is 68 percent.
EXAMPLE 2 ZnCl alone2Effect of solutions on alpha-glucosidase inhibitory Activity
Respectively preparing ZnCl with the concentration of 0.1-0.5mmol/L2Solution, measuring the inhibition rate of metal solution with different concentrations on alpha-glucosidaseWith ZnCl, as shown in FIG. 22The increasing concentration of the solution gradually increases the inhibition rate to alpha-glucosidase, which indicates that ZnCl alone is used2The solution has effect in inhibiting alpha-glucosidase.
Example 3 preparation of Porphyra tenera enzymatic hydrolysate alpha-glucosidase inhibitory active polypeptide Zinc chelate
Dissolving 0.18g laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide in 30mL ZnCl with the concentration of 0.5mmol/L2The solution is prepared, and the concentration of the laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide in the solution is 6 mg/ml. Adjusting the pH value of the solution to 4.5, and then placing the solution in a shaking water bath shaker at 37 ℃ for reaction for 1.5h to obtain the laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide zinc chelate. The degree of chelation was found to be 25.6%. The product was prepared as a 1mg/ml solution, and its α -glucosidase inhibition was determined as described above in the specification, which was 79.8%.
Example 4 preparation of Porphyra tenera enzymatic hydrolysate alpha-glucosidase inhibitory active polypeptide iron chelate
Dissolving 0.09g of laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide in 30mL of FeCl with the concentration of 0.5mmol/L2The concentration of the laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide in the solution is 3mg-1. Adjusting the pH value of the solution to 5, and then placing the solution in a shaking water bath shaker at 60 ℃ for reaction for 2 hours to obtain the laver enzymolysis product alpha-glucosidase inhibitory active polypeptide iron chelate. The chelating degree of the chelating polypeptide is determined to be 29.8 percent, and the product is prepared into 1mg.mL-1The alpha-glucosidase inhibition of the concentrated solution was measured by the method described in the above specification, and found to be 82.78%.
Example 5 in vitro simulation of gastrointestinal stability
Gastrointestinal digestion is divided into two stages, gastric digestion and duodenal digestion. The gastrointestinal stability of the laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide zinc chelate prepared by the invention is simulated in vitro according to the following method:
gastric digestion stage: quantitatively prepare 1mg.mL-1And the pH is adjusted to 2.0(1M HCl). Incubating at 37 deg.C for 15min, addingPepsin with different masses was shaken at a constant temperature of 37 ℃ for a certain time, the pH was adjusted to 7.0(5M NaOH), and the pepsin reaction was stopped. Duodenum digestion stage: placing the chelated polypeptide solution subjected to the gastric digestion stage at the constant temperature of 37 ℃ for incubation for 15min, adding trypsin according to different mass ratios of the alpha-glucosidase inhibitory peptide-Zn chelate and the enzyme, and continuing to shake for a certain time at the constant temperature of 37 ℃. Keeping the temperature at 85 ℃ for 20min, and stopping the digestion reaction of duodenum. The alpha-glucosidase inhibitory activity was measured at the gastric digestion stage and the duodenal digestion stage, respectively. FIGS. 3-4 show the time and quality stability of the product in the gastric and duodenal digestion stages, respectively, and it can be seen that the alpha-glucosidase inhibition rate of the product is not substantially changed during the digestion time, and the results show that: the laver enzymolysis product alpha-glucosidase inhibitory activity polypeptide zinc chelate has good gastrointestinal stability.
The above description is only a preferred embodiment of the present invention and is not intended to limit the present invention, it should be noted that, for those skilled in the art, many modifications and variations can be made without departing from the technical principle of the present invention, and these modifications and variations should also be regarded as the protection scope of the present invention.

Claims (8)

1. A method for preparing active peptide metal chelate by laver enzymolysis is characterized by comprising the following steps:
(1) performing enzymolysis reaction on the crushed laver and protease in a buffer solution, and centrifuging and taking supernatant after the enzymolysis is finished; the protease consists of alkaline protease, neutral protease and aminopeptidase; the content of the alkaline protease is 7 x 104-9×104U.g-1Thallus Porphyrae with neutral protease content of 7 × 104-9×104U.g-1Thallus Porphyrae with aminopeptidase content of 25-30U.g-1Laver; the laver is Porphyra yezoensis;
(2) filtering the supernatant obtained in the step (1), concentrating and drying the filtrate to obtain solid polypeptide powder;
(3) dissolving the solid polypeptide powder obtained in the step (2) in a metal salt aqueous solution to perform a chelation reaction, wherein the pH value of the chelation reaction is 4.0-5.0, and the temperature is 35-40 ℃, so as to obtain the laver enzymatic hydrolysis active peptide metal chelate; the metal salt is zinc chloride, zinc nitrate or ferrous chloride.
2. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1, wherein: in the step (1), the temperature of the enzymolysis reaction is 45-55 ℃.
3. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1, wherein: in the step (1), the pH of the buffer solution is 8.0 to 9.0.
4. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1 or 3, wherein: in the step (1), the buffer solution is phosphate buffer solution or Tris-HCl buffer solution.
5. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1 or 3, wherein: in the step (1), the mass-to-volume ratio of the laver to the buffer solution is 1:30-1:35 g/ml.
6. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1, wherein: in the step (2), an ultrafiltration membrane with the molecular weight cutoff of 10kDa-30kDa and a nanofiltration membrane with the molecular weight cutoff of 500Da-1kDa are used for filtering in sequence.
7. The method for preparing an active peptide metal chelate by enzymatic hydrolysis of laver according to claim 1, wherein: in the step (3), the mass ratio of the solid polypeptide powder to the metal salt is 6:1-24: 1.
8. The use of a laver enzymolysis active peptide metal chelate prepared by the method of claim 1 in the preparation of an alpha-glucosidase inhibitor.
CN201610980350.8A 2016-11-08 2016-11-08 Method for preparing active peptide metal chelate by laver enzymolysis Active CN106755227B (en)

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CN104293749B (en) * 2014-10-11 2017-01-11 江南大学 Method for preparing high-yield leucine aminopeptidase through fermentation of recombinant bacillus subtilis
CN104628824B (en) * 2015-02-09 2017-08-11 福州大学 One main laver metal-chelating protein peptide and preparation method thereof

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