CN112680491A - Method for preparing high-F-value oligopeptide from maize yellow powder - Google Patents
Method for preparing high-F-value oligopeptide from maize yellow powder Download PDFInfo
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- CN112680491A CN112680491A CN201910987553.3A CN201910987553A CN112680491A CN 112680491 A CN112680491 A CN 112680491A CN 201910987553 A CN201910987553 A CN 201910987553A CN 112680491 A CN112680491 A CN 112680491A
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- flavourzyme
- bacillus natto
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Abstract
The invention discloses a preparation method of a high F value active peptide, belonging to the technical field of corn protein deep processing. The method comprises the steps of taking corn gluten as a raw material, taking bacillus natto as a protease production strain, performing enzymolysis on corn protein by using a fermentation crude enzyme solution with high enzyme activity obtained after fermentation for 45 hours to obtain a preliminary enzymolysis product, performing sequential enzymolysis on the product by using flavourzyme, adsorbing and dearomatizing by using activated carbon, and finally performing separation, purification and freeze drying on the treated product to obtain the high-F-value active peptide finished product. The invention can improve the utilization rate of the maize yellow powder, the oligopeptide content in the enzymolysis liquid reaches 17.8mg/ml, the protein utilization rate reaches 53 percent, and meanwhile, the F value of the adsorbed oligopeptide reaches 24. The invention has mild technical action condition, more retains the biological activity of the prepared active peptide with high F value and other functional components contained in the raw material, and has good application prospect.
Description
Technical Field
The invention relates to a method for preparing a high-F-value oligopeptide from corn gluten, belonging to the technical field of deep processing of corn protein.
Background
Corn is one of three major food crops in the world and is an important feed raw material, and has high yield per unit and great yield increasing potential, so the corn plays an important role in agricultural production. The corn protein can be used for extracting excellent products such as zein, corn yellow pigment, glutamic acid and the like, and can also be used for preparing corn active peptides with various physiological functions, such as corn protein peptide, high F value oligopeptide, antihypertensive peptide and the like, so that the additional value of corn processing is greatly improved. Although the application range of corn is wide, people mainly utilize the corn for a long time to produce starch, and the corn protein resource is wasted greatly. For this reason, some developed countries in the world are actively engaged in research for developing and utilizing new approaches to zein.
In China, more than 600 corn wet starch plants exist in China mainly for extracting starch, the production capacity accounts for 80% of the national starch yield, only 65% of the corn is utilized for starch production, and other parts enter byproducts. The corn is produced and consumed by 700 million tons of corn and 200 million tons of corn protein powder (commonly called yellow powder) every year in China, and the corn protein powder contains about 60 percent of protein, mainly comprising alcohol soluble protein (68 percent), glutelin (22 percent), globulin (2 percent) and albumin. From a nutritional point of view, zein has a very unbalanced amino acid content, and in particular, the essential amino acids lysine and tryptophan are relatively lacking, so that the value is low, and the application of the zein is limited. For a long time, the corn protein powder can only be sold as feed at low price or naturally discharged, and the corn protein discharged along with waste liquid in China is as high as 8 ten thousand tons every year, thereby not only polluting the environment, but also causing the waste of protein resources.
Because the corn protein has special protein amino acid composition, the content of three branched chain amino acids (BCAA: Val, lie, Leu) is higher, and the content of aromatic amino acids (AAA: Tyr, Phe, Trp) is lower, the corn oligopeptide mixture with high F value can be prepared by in vitro hydrolysis, adjusting the peptide fragment length of the product and reducing the generation of free amino acids. The high F value oligopeptides refer to oligopeptides with the ratio of branched chain amino acid to aromatic amino acid higher than 20 and the number of peptide chain amino acid less than 9. Due to the characteristics of unique amino acid composition ratio (high BACC and low AAA) and easy absorption and utilization by human bodies, the compound has a plurality of active and effective physiological functions, and is greatly helpful for clinically and auxiliarily treating hepatic encephalopathy and phenylketonuria, improving the nutritional state of postoperative patients, daily health care, liver protection, fatigue resistance and the like.
Disclosure of Invention
The invention aims to provide a method for preparing high F value oligopeptide, which uses fermentation products of bacillus natto and flavourzyme to carry out enzymolysis on raw materials containing zeaxanthin powder; the fermentation product of the bacillus natto contains alkaline protease not less than 50U/mL and neutral protease not less than 100U/mL, and the addition amount of the flavourzyme is 20000-25000U/g of maize yellow powder.
In one embodiment of the invention, the Bacillus natto (Bacillus natto) is Bacillus natto CICC10023, which is purchased from China center for Industrial culture Collection of microorganisms.
In one embodiment of the invention, the fermentation product of the bacillus natto is natto protease, and is obtained by fermenting at the temperature of 35-39 ℃, the pH value of 8.5-9.5 and the rotating speed of 180-220 r/min and centrifuging for 20min at 8000 r/min.
In one embodiment of the invention, the components of the culture medium for fermenting the bacillus natto are as follows: 8-10 g/L of glucose, 15-20 g/L of fish meal peptone, 1-2 g/L of calcium chloride and 1-2 g/L of magnesium sulfate.
In one embodiment of the invention, the enzymatic hydrolysis is performed with nattokinase first and then flavourzyme.
In one embodiment of the invention, the natto protease is added according to the ratio of 5000-7500U of the natto protease/g of the corn gluten meal, and enzymolysis is carried out for 4-6 hours under the conditions of 50-55 ℃ and pH of 8.0-10.0.
In one embodiment of the invention, the flavourzyme is added according to 20000-25000U/g of maize yellow powder, and enzymolysis is carried out for 4-6 h under the conditions of 40-55 ℃ and pH 6.5-7.5.
In one embodiment of the present invention, the raw material containing the zeaxanthin powder is pretreated as follows: mixing the raw materials in a ratio of 1: 5-1: 12, adding the corn gluten meal into PBS buffer solution with the pH value of 5.0-6.0, adding 150-200U/g of medium-temperature alpha-amylase, performing heat preservation and enzymolysis at 55-60 ℃ for 4-6 h, inactivating enzyme at 100 ℃ for 10min, adding a sodium sulfite reducing agent with the concentration of 0.5-0.7 mg/ml, heating at the temperature of 115-125 ℃ for 1.5-2.5 h, washing, drying and crushing to obtain the pretreated zein.
In one embodiment of the present invention, the reaction solution after the enzymatic hydrolysis of flavourzyme is subjected to adsorption dearomatization.
In one embodiment of the invention, the dearomatization is a 1: 10-1: 15, adding activated carbon, and adsorbing for 2 hours at the temperature of 40-55 ℃ and the pH value of 2.0-3.0.
In one embodiment of the invention, the method comprises the steps of:
(1) mixing the raw materials in a ratio of 1: 5-1: 12, adding the corn gluten meal into a PBS (phosphate buffer solution) with the pH value of 5.0-6.0 at a solid-to-liquid ratio, adding a sodium sulfite reducing agent with the concentration of 0.5-0.7 mg/ml, heating at the temperature of 115-125 ℃ for 1.5-2.5 h, adding medium-temperature alpha-amylase at the concentration of 150-200U/ml, carrying out heat preservation and enzymolysis at the temperature of 55-60 ℃ for 4-6 h, carrying out water bath enzyme deactivation at the temperature of 100 ℃ for 10min after the enzymolysis is finished, and finally washing, drying and crushing to obtain the pretreated zein;
(2) selecting bacillus natto as a protease fermentation strain, wherein the fermentation condition is that the temperature is 35-39 ℃, the pH is 8.5-9.5, the rotating speed of a shaking table is 180-220 r/min, the inoculation amount is 5-6%, the fermentation medium is 8-10 g/L of glucose, 15-20 g/L of fish meal peptone, 1-2 g/L of calcium chloride and 1-2 g/L of magnesium sulfate, and fermenting for 45-48 h to obtain fermentation liquor containing the natto protease, wherein the alkaline protease is not lower than 50U/ml, and the neutral protease is not lower than 100U/ml;
(3) centrifuging the fermentation liquor obtained in the step (2) for 20min at 8000r/min, and removing thalli and impurities to obtain natto protease with the enzyme activity of 200-300U/mL;
(4) performing enzymolysis on the corn protein in the step (1) by using the natto protease in the step (3), performing enzymolysis for 4-6 h at 50-55 ℃ and pH of 8.0-10.0 by using the addition amount of 5000-7500U of natto protease/g of corn gluten meal, finally putting the corn gluten meal into boiling water for inactivating enzyme for 10min, centrifuging for 20min at 8000r/min, removing insoluble protein, and taking out supernatant to obtain natto protease enzymolysis liquid;
(5) and (3) carrying out enzymolysis on the enzymolysis liquid obtained in the step (4) by using flavourzyme, adding flavourzyme into the maize yellow powder at 20000-25000U/g, carrying out enzymolysis for 4-6 h at 40-55 ℃ and under the condition that the pH value is 6.5-7.5, centrifuging for 10min at 8000r/min, removing impurities, and obtaining the enzymolysis liquid obtained after two-step enzymolysis.
(6) And (3) adsorbing and dearomatizing the enzymatic hydrolysate in the step (5) by using activated carbon, wherein the ratio of the activated carbon to the enzymatic hydrolysate in the adsorption process is 1: 10-1: 15, adding modified activated carbon into the carbon solution, adsorbing for 2-2.5 hours at the temperature of 20-25 ℃ and under the condition of pH 2.0-3.0, and finally filtering to obtain the high-F-value oligopeptide adsorption solution.
(7) Freeze-drying the high F value oligopeptide obtained in the step (6) into powder at-80 ℃.
Has the advantages that: the invention takes maize yellow powder as a raw material to prepare maize protein, takes bacillus natto as a protease production strain, utilizes fermentation crude enzyme liquid of the bacillus natto to carry out enzymolysis on the maize protein, uses flavourzyme to carry out sequential enzymolysis on enzymolysis products, then uses activated carbon to adsorb and remove aromatic substances, and obtains a finished product of the active peptide with high F value through freeze drying. The invention can not only make full use of the maize yellow powder, the oligopeptide content in the enzymolysis liquid reaches 17.8mg/ml, the protein conversion rate can reach 53 percent, and the F value of the adsorbed oligopeptide reaches more than 24.
Drawings
FIG. 1 shows the hydrolysis effect of nattokinase at different temperatures.
FIG. 2 shows the hydrolysis effect of nattokinase at different pH values.
FIG. 3 shows F values of hydrolysates at different levels of flavourzyme added.
FIG. 4 shows F values of the hydrolyzed solutions at different amounts of acidic protease added.
FIG. 5 shows F values of hydrolysates with different amounts of carboxypeptidase added.
Detailed Description
Protease activity determination: determination by Folin phenol method
Drawing a standard curve: taking 6 test tubes, respectively sucking 1.0mL (0, 20, 40, 60, 80, 100 mu g/mL) of tyrosine with different concentrations according to the serial numbers of tables 1-2, respectively adding 5.0mL of 0.4M sodium carbonate, respectively adding 1.0mL of diluted formalin reagent, shaking uniformly and placing in a water bath kettle. And (3) carrying out heat preservation and color development at 40 ℃ for 20min, then measuring the OD value at 680nm by using an ultraviolet spectrophotometer, and drawing a standard curve by taking the net OD value as a vertical coordinate and the concentration of tyrosine as a horizontal coordinate.
Taking 2mL of fermentation liquor, centrifuging at 8000r/min for 10min, and obtaining supernatant as crude enzyme liquid. The crude enzyme solution can be diluted with a borate buffer solution with pH 10.5 according to the estimated enzyme activity.
Taking 1mL of diluted enzyme solution, placing in a test tube, keeping the temperature at 40 ℃ for 2min, adding 1mL of casein solution preheated at 40 ℃ for 5min, shaking, mixing, and rapidly placing in a 40 ℃ constant-temperature water bath kettle. Accurately timing, keeping the temperature for reaction for 10min, immediately adding 2mL of 10% trichloroacetic acid, and shaking up to terminate the reaction. Taking out and standing for 10min, and centrifuging at 10000r/min for 10min to remove unreacted casein precipitate. Taking 1mL of supernatant, adding 5mL of 0.4mol/L sodium carbonate solution and 1mL of 33% formalin reagent in sequence, mixing uniformly immediately, placing in a constant temperature water bath kettle at 40 ℃ for heat preservation and color development for 20min, and adjusting to zero at the wavelength of 680nm to measure the absorbance A.
For the blank, 2mL of 10% trichloroacetic acid was added immediately after the enzyme solution was added, and the mixture was mixed to inactivate the enzyme. After incubation for 20min, 1mL of casein solution was added. Then the same enzyme solution sample was run.
Calculating enzyme activity: u ═ 10 (axk × 4 × N)/10
In the formula: a- - - -absorbance measured at 680 nm; k-inverse of the slope of the tyrosine standard curve; 4- -total volume of reaction reagents; n- - -dilution factor of the enzyme solution; 10- -time of reaction; three replicates were made each time and the average was taken.
And (3) measuring the content of the peptide: measurement by biuret method.
Preparation of biuret reagent
a) NaOH solution: 6g of NaOH is weighed by a beaker, 25ml of distilled water is weighed and added into the beaker to dissolve the NaOH, and the concentration of the NaOH is prepared to be 6mol/L for standby.
b) Biuret reagent: balanceTaking 0.75g of copper sulfate (CuSO)4·5H2O) was dissolved in freshly prepared 500ml of distilled water, 2.25g of sodium potassium tartrate (KNaC) was added4H4O6·4H2O (for bonding Cu)2+For preventing CuO from precipitating under alkaline conditions) and 1.5g of KI (for preventing alkaline copper tartrate from auto-reducing and for preventing Cu from being added2Isolation of O), until complete dissolution, 25ml of 6g/L NaOH solution was added with stirring and the volume was made 250ml with water, and the mixture was placed in a plastic bottle and tightly covered for storage.
Taking ten 10ml volumetric flasks, preparing 0.0, 0.2, 0.4, 0.6, 0.8, 1.0, 1.2, 1.4, 1.6 and 1.8mg/ml Gly-Gly-Tyr-Arg tetrapeptide standard solutions by using 5% TCA in sequence, then respectively taking 6.0ml standard solutions, adding 4.0ml biuret reagent, uniformly mixing, standing for 10min, centrifuging at 2000r/min for 10min, taking supernate, and measuring OD value at 540nm (taking a first tube as a blank control). A standard curve was prepared with the peptide concentration as abscissa X (mg/ml) and the OD value as ordinate Y.
The method comprises the following steps: taking 2.5ml of sample solution, adding 2.5ml of 10% (W/V) trichloroacetic acid (TCA) aqueous solution, uniformly mixing on a vortex mixer, standing for 10min, centrifuging for 15min at 4000r/min, transferring all supernate into a 50ml volumetric flask, fixing the volume to the scale by using 5% TCA, and uniformly shaking. Then 6.0ml of the solution is put into another test tube, 4.0ml of biuret reagent (sample solution: biuret reagent is 3:2, V/V) is added into the test tube, the mixture is uniformly mixed on a vortex mixer, the mixture is kept stand for 10min, the mixture is centrifuged at 2000r/min for 10min, the supernatant is taken and the OD value is measured under 540nm, the polypeptide concentration C (mg/ml) in the sample solution is obtained by contrasting a standard curve, and the polypeptide content in the sample can be further obtained.
F value determination of the enzymolysis liquid: centrifuging the adsorption solution at 10000r/min for 10min, taking out the supernatant, and detecting amino acid components by using high-efficiency solution relative to the supernatant by adopting an OPA derivation method.
Determination of molecular weight distribution: centrifuging the fermentation liquid at 8000r/min for 10min, collecting the fermentation supernatant peptide liquid, and detecting the molecular weight distribution of the adsorption liquid by HPLC.
Protein conversion rate:
in the formula: the protein content was 83.1%.
Example 1
(1) Mixing the raw materials in a ratio of 1: adding corn gluten meal into PBS buffer solution with pH of 5.2 at a solid-to-liquid ratio of 10, adding 165U/ml of medium-temperature alpha-amylase, keeping the temperature and performing enzymolysis for 4 hours at 57 ℃, inactivating the enzyme for 10 minutes in 100 ℃ water bath after the enzymolysis is finished, adding a sodium sulfite reducing agent with the concentration of 0.7mg/ml, heating at 120 ℃ for 2.0 hours, and finally washing, drying and crushing to obtain the pretreated zein;
(2) taking bacillus natto as a protease fermentation strain, fermenting at 37 ℃, pH 9.0, shaking table rotating speed of 180-220 r/min and inoculum size of 5%, wherein a fermentation medium is 10g/L of glucose, 20g/L of fish meal peptone, 1g/L of calcium chloride and 1g/L of magnesium sulfate, and taking out after fermenting for 45-48 h;
(3) centrifuging the fermentation liquor obtained in the step (2) for 20min at 8000r/min, and removing thallus and impurities to obtain natto protease;
(4) measuring the enzyme activity of the natto protease in step (3), wherein the alkaline protease is 50-60U/ml, and the neutral protease is 100-130U/ml;
(5) performing enzymolysis on the corn protein in the step (1) by using the natto protease in the step (4), performing enzymolysis for 4 hours at the enzyme concentration of 200U/ml and the pH value of 9.0 at 55 ℃, wherein the hydrolysis degree of the corn protein is 24%, finally putting the corn protein into boiling water for inactivating enzyme for 10min, centrifuging for 20min at 8000r/min, removing insoluble protein, and taking out supernatant to obtain natto protease enzymolysis liquid;
(6) determining the amino acid components of the enzymolysis liquid in the step (5), wherein the F value is 3.4;
(7) and (3) adsorbing and dearomatizing the enzymatic hydrolysate in the step (6) by using activated carbon, wherein the ratio of the activated carbon to the enzymatic hydrolysate in the adsorption process is 1: 10, adding modified activated carbon, adsorbing for 2 hours at the temperature of 20-25 ℃ and under the condition of pH 2.0-3.0, and finally filtering to obtain an adsorption solution.
(8) And (3) detecting the molecular weight distribution and the F value of the adsorption solution in the step (7), wherein the oligopeptide less than 1000Da is more than 80%, and the F value is more than 24.
Example 2
The specific implementation manner is the same as that in example 1, except that the enzymolysis temperature in the step (5) is adjusted to 35 ℃, 40 ℃, 45, 50 and 55 ℃, and the result is shown in fig. 1, and the hydrolysis degree of enzymolysis is 10-15% within 4-6 h at 45-55 ℃.
Example 3
The specific implementation manner is the same as that in example 1, except that the pH in the enzymolysis process in step (5) is respectively adjusted to 7, 7.5, 8, 8.5 and 9, and the result is shown in fig. 2, and the hydrolysis degree reaches 8-12% in 4-6 h of enzymolysis under the pH range of 8.0-9.0.
Example 4
The specific implementation manner is the same as example 3, except that the flavourzyme of 10000, 15000, 20000, 25000 and 30000U/g of corn gluten is added to the enzymolysis solution treated in the step (6) for enzymolysis for 4 hours, and as shown in fig. 3, the F value after activated carbon adsorption reaches 10-15 under the addition amount of 20000-25000U/g of corn gluten, and when the addition amount is 20000U/g of corn gluten, the F value is improved by nearly 4 times than that of example 1.
Example 5
On the basis of example 4, the enzymolysis temperature of the flavourzyme is respectively adjusted to 40, 45, 50, 55 and 60 ℃, and the adding amount of the flavourzyme is 20000U/g maize yellow powder. When the temperature is 40 ℃, the content of amino nitrogen in the enzymolysis liquid is 1.75 mg/mL-1(ii) a The amino acid nitrogen content reaches 1.85mg/mL at 45 deg.C, and the amino acid nitrogen content reaches 1.9 mg/mL at maximum when the temperature is increased to 50 deg.C-1(ii) a The amino nitrogen content gradually decreases as the temperature continues to increase.
Example 6
On the basis of example 4, the enzymolysis temperature of the flavourzyme is controlled to be 50 ℃, and the adding amount of the flavourzyme is 20000U/g maize yellow powder. The initial pH of the flavourzyme enzymolysis was adjusted to 6.0, 6.5, 7.0, 7.5 and 8, respectively. The result shows that when the initial pH is 6-6.5, the content of amino nitrogen reaches more than 1.8; when the initial pH is 6.5, the amino nitrogen content in the enzymolysis liquid reaches the maximum 1.88 mg.mL-1(ii) a The initial pH is continued to increase and the amino nitrogen content gradually decreases.
Example 7
According to the steps of the example 1, after the step (6), adding flavourzyme according to the adding amount of 20000U/g of maize yellow powder, carrying out enzymolysis for 4 at the temperature of 50 ℃ and the pH value of 6.5, centrifuging for 10min at 8000r/min, and removing impurities to obtain enzymolysis liquid after two-step enzymolysis. And (3) adsorbing and dearomatizing the enzymatic hydrolysate in the step (6) by using activated carbon, wherein the ratio of the activated carbon to the enzymatic hydrolysate in the adsorption process is 1: adding modified active carbon into the carbon solution of 10, adsorbing for 2 hours at the temperature of 25 ℃ and under the condition of pH 2.5, and finally filtering to obtain an adsorption solution.
The molecular weight and content of the oligopeptides prepared in example 1 and example 7 were measured, respectively, and the results are shown in table 1.
As shown in Table 1, after the enzymolysis is carried out by flavourzyme, the ratio of oligopeptide (2-9 amino acids) with the molecular weight of 200-1000 Da in an enzymolysis product is increased from 66.39% to 71.19%; the ratio of free amino acid with molecular weight less than 200Da is increased from 19.84% to 22.02%; the proportion of macromolecular peptides with molecular weight >1000Da is reduced from 13.87% to 6.79%. The result shows that after the sequential enzymolysis of flavourzyme, macromolecular peptides with the molecular weight more than 1000Da in the natto protein enzymolysis product are further hydrolyzed, and simultaneously, more free amino acids are generated.
TABLE 1 molecular weight distribution of different enzymatic products
Comparative example 1
The specific implementation manner is the same as that in example 1, except that 0.2, 0.4, 0.6, 0.8 and 1% by mass of acid protease (the enzyme activity of the acid protease is 5000U/g) is added to the enzymolysis solution treated in the step (6), and as shown in fig. 4, when the addition amount is in the range of 0.1-0.8%, the F value after activated carbon adsorption reaches 9-10, which is improved by less than 3 times than before adsorption.
Comparative example 2
The specific implementation manner is the same as that in example 1, except that 0.02, 0.04, 0.06, 0.08 and 0.12% by mass of carboxypeptidase (the enzyme activity of the carboxypeptidase is 2500U/g) is added into the enzymolysis liquid treated in the step (6), and as shown in fig. 5, when the addition amount is in the range of 0.02-0.12%, the F value after activated carbon adsorption reaches 10-15, which is improved by less than 4 times than before adsorption.
Comparative example 3
The method takes bacillus natto as a fermentation strain and maize yellow powder as a raw material for fermentation, and comprises the following specific steps:
(1) mixing the raw materials in a ratio of 1: adding corn gluten meal into PBS buffer solution with pH of 5.2 at a solid-to-liquid ratio of 10, adding 165U/ml of medium-temperature alpha-amylase, keeping the temperature and performing enzymolysis for 4 hours at 57 ℃, inactivating the enzyme for 10 minutes in 100 ℃ water bath after the enzymolysis is finished, adding a sodium sulfite reducing agent with the concentration of 0.7mg/ml, heating at 120 ℃ for 2.0 hours, and finally washing, drying and crushing to obtain the pretreated zein;
(2) inoculating bacillus natto serving as a fermentation strain into the corn protein treated in the step (1) according to the proportion of 4%, and fermenting for 45-48 hours at the temperature of 37 ℃, the pH value of 9.0 and the corn protein substrate concentration of 40 g/L;
(3) determining the amino acid component of the fermentation liquor in the step (2), wherein the F value is 3.3;
(4) and (3) carrying out enzymolysis on the fermentation liquor in the step (3) by using flavourzyme, adding the flavourzyme into 20000U/g of soluble protein, carrying out enzymolysis for 4h at 55 ℃ and pH 6.5, centrifuging for 10min at 8000r/min, and removing impurities to obtain an enzymolysis liquid.
(5) Determining the amino acid components of the enzymolysis liquid in the step (4), wherein the F value is 3.9;
(6) and (3) adsorbing and dearomatizing the enzymatic hydrolysate in the step (5) by using activated carbon, wherein the ratio of the activated carbon to the enzymatic hydrolysate in the adsorption process is 1: 10, adding modified activated carbon, adsorbing for 2 hours at the temperature of 20-25 ℃ and under the condition of pH 2.0-3.0, and finally filtering to obtain an adsorption solution.
(7) And (4) detecting the molecular weight distribution and the F value of the adsorption solution in the step (9), wherein the oligopeptide content of less than 1000Da is 70%, and the F value is 7.6.
Comparative example 4
The specific implementation mode is the same as that of example 1, except that commercial alkaline protease and neutral protease are adopted to replace bacillus natto fermentation liquor, amino acid components after enzymolysis are detected, and the result shows that the F value is 4.1; the result of adsorption using activated carbon showed 16.8.
Comparative example 5
The specific implementation mode is the same as that of example 1, except that the flavor protease is firstly adopted for enzymolysis, then the bacillus natto fermentation liquor is adopted for enzymolysis, the amino acid components after enzymolysis are detected, and the result shows that the F value is 3.3; the result of adsorption using activated carbon showed 9.6.
Although the present invention has been described with reference to the preferred embodiments, it should be understood that various changes and modifications can be made therein by those skilled in the art without departing from the spirit and scope of the invention as defined in the appended claims.
Claims (10)
1. A method for preparing high F value oligopeptide is characterized in that a fermentation product of Bacillus natto and flavourzyme are used for enzymolysis of a raw material containing zeaxanthin powder; the fermentation product of the bacillus natto contains alkaline protease more than or equal to 50U/mL and neutral protease more than or equal to 100U/mL, and the addition amount of the flavourzyme is 20000-25000U/g of maize yellow powder.
2. The method of claim 1, wherein the Bacillus natto is Bacillus natto CICC 10023.
3. The method according to claim 1 or 2, wherein the fermentation product of the bacillus natto is a nattokinase obtained by the bacillus natto under the condition that the temperature is 35-39 ℃ and the pH is 8.5-9.5.
4. The method according to claim 1, wherein the enzymatic hydrolysis is carried out with a nattokinase and then with a flavourzyme.
5. The method according to claim 1 or 4, wherein the nattokinase is subjected to enzymolysis for 4 to 6 hours at the temperature of 50 to 55 ℃ and the pH value of 8.0 to 10.0.
6. The method according to claim 1 or 5, wherein the flavourzyme is added at 20000-25000U/g maize yellow powder and is subjected to enzymolysis for 4-6 hours at 40-55 ℃ and pH 6.5-7.5.
7. The method according to any one of claims 1 to 6, wherein the reaction solution after the enzymatic hydrolysis is dearomatized.
8. The process according to claim 7, characterized in that it is carried out with activated carbon or via HCl/HNO3The modified active carbon is used for adsorption and dearomatization.
9. A high F value oligopeptide prepared by the method of any one of claims 1 to 8.
10. Use of the high F value according to claim 9 for the preparation of food, pharmaceutical, health care products.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113403361A (en) * | 2021-06-11 | 2021-09-17 | 江南大学 | Preparation method of high-value active oligopeptide |
| CN114805471A (en) * | 2022-03-17 | 2022-07-29 | 南京工业大学 | high-F-value oligopeptide of fructus cannabis seed meal, preparation method of oligopeptide and application of oligopeptide in increasing yield of nattokinase |
| CN116035214A (en) * | 2022-04-24 | 2023-05-02 | 哈尔滨拓百世生物科技有限责任公司 | Preparation method of food additive nano selenium sol |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1570127A (en) * | 2003-07-23 | 2005-01-26 | 东北农业大学 | High F value oligopeptide production method by corn protein enzymolysis |
| CN1733928A (en) * | 2005-08-09 | 2006-02-15 | 吉林农业大学 | Corn protein high F value oligopeptide production method |
| CN102021216A (en) * | 2010-11-11 | 2011-04-20 | 湖北远成药业有限公司 | Extraction method of antialcoholism peptide |
| CN106349742A (en) * | 2016-08-30 | 2017-01-25 | 杭州上拓环境科技股份有限公司 | Membrane treatment system for extracting corn peptide and corn yellow pigment and treatment technology |
| CN109731547A (en) * | 2019-01-29 | 2019-05-10 | 江南大学 | A kind of efficient absorption takes off the modified activated carbon and preparation method thereof of virtue |
-
2019
- 2019-10-17 CN CN201910987553.3A patent/CN112680491A/en active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1570127A (en) * | 2003-07-23 | 2005-01-26 | 东北农业大学 | High F value oligopeptide production method by corn protein enzymolysis |
| CN1733928A (en) * | 2005-08-09 | 2006-02-15 | 吉林农业大学 | Corn protein high F value oligopeptide production method |
| CN102021216A (en) * | 2010-11-11 | 2011-04-20 | 湖北远成药业有限公司 | Extraction method of antialcoholism peptide |
| CN106349742A (en) * | 2016-08-30 | 2017-01-25 | 杭州上拓环境科技股份有限公司 | Membrane treatment system for extracting corn peptide and corn yellow pigment and treatment technology |
| CN109731547A (en) * | 2019-01-29 | 2019-05-10 | 江南大学 | A kind of efficient absorption takes off the modified activated carbon and preparation method thereof of virtue |
Non-Patent Citations (4)
| Title |
|---|
| 张振洋: "玉米高F值寡肽的微生物发酵法生产制备", 《中国优秀硕士学位论文全文数据库工程科技Ⅰ辑》 * |
| 无锡轻工大学 等: "《21世纪的食品——食品与资源 技术 环境》", 31 October 2000, 中国轻工业出版社 * |
| 郑明洋: "玉米高F值寡肽的制备及生理功能研究", 《中国优秀硕士学位论文全文数据库工程科技Ⅰ辑》 * |
| 高瑞雄 等: "冷榨核桃粕液态发酵制备核桃多肽", 《食品科学》 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113403361A (en) * | 2021-06-11 | 2021-09-17 | 江南大学 | Preparation method of high-value active oligopeptide |
| CN113403361B (en) * | 2021-06-11 | 2024-01-26 | 江南大学 | Preparation method of high-value active oligopeptide |
| CN114805471A (en) * | 2022-03-17 | 2022-07-29 | 南京工业大学 | high-F-value oligopeptide of fructus cannabis seed meal, preparation method of oligopeptide and application of oligopeptide in increasing yield of nattokinase |
| CN116035214A (en) * | 2022-04-24 | 2023-05-02 | 哈尔滨拓百世生物科技有限责任公司 | Preparation method of food additive nano selenium sol |
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