CN103923964A - Method for preparing casein hydrolysate with stable functionality by using different hydrolysis conditions - Google Patents
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Abstract
The invention provides a method for preparing casein hydrolysate with stable functionality by using different hydrolysis conditions, and belongs to the fields of casein hydrolysis technology and processing. The method comprises the following steps: firstly selecting a substrate (casein)-enzyme (alkaline protease) serving as a reaction system, controlling the constancy of pH in a hydrolytic process by using a pH-stat method, changing three hydrolysis conditions, namely temperature (T), enzyme-to-substrate ratio (E/S) and substrate concentration (S) in a certain range, and when hydrolysate reaches established degree of hydrolysis (DH), carrying out enzyme deactivation drying, wherein the properties of the obtained hydrolysate with the same degree of hydrolysis have no significant difference, namely the obtained hydrolysate is stable. According to the method, the hydrolysate with the same degree of hydrolysis is obtained by adjustment according to different production conditions and hydrolysis, so that the hydrolysate has identical properties. The method can be used for guiding industrial production; the production conditions are flexibly changed; and the stability of the products still can be ensured.
Description
Technical field
The present invention relates to a kind of method than combination preparation at the bottom of different hydrolysis temperatures, enzyme with the hydrolysate of specific function character of utilizing, belong to casein hydrolysis technology manufacture field.
Background technology
Proteolytic enzyme is the one that belongs to lytic enzyme, and it is mainly the peptide bond of protein hydrolysate and polypeptide.According to the source of enzyme, proteolytic enzyme can be divided into protein for animal enzyme, plant origin proteolytic enzyme, microbe-derived proteolytic enzyme.According to the difference of the position of catalysis, proteolytic enzyme can be divided into endopeptidase and exopeptidase.Endopeptidase is nowadays to use more enzyme, and endopeptidase can be divided into serine protease, L-Cysteine HCL Anhydrous, these four kinds, metalloprotease and l-asparagine proteolytic enzyme according to the difference of the avtive spot of effect again.The mankind just used proteolytic enzyme before the centuries, and typical example is Chinese fermented bean products.In the last few years, proteolytic enzyme, due to its numerous advantage, was more and more used in the middle of industrial production and experimental study.People more and more use protease hydrolysis different kinds of proteins, to improving its structure and function, as improve emulsifying property, whipability, solvability of soybean protein etc.; Or preparing some has as the peptide material of oxidation-resistance, the special physiological function such as hypotensive.These researchs are to be all often based upon the different enzyme of research to a certain substrate, or the effect of a certain enzyme to multiple substrate, are hydrolyzed the different time or reach different degree of hydrolysis, to obtain the hydrolysising condition of optimization or the degree of hydrolysis through optimizing.
For casein, well-known, it is that milk is met a kind of albumen polymer generating after acid.Casein accounts for 80% of Tot Prot in milk, accounts for 3% of its quality, is also the main component of cheese.Casein is that iso-electric point is the bisexual protein of pH4.6, it is the mixture of multiple (approximately 20 kinds) phosphorprotein (phosphoproteins) of bovine mammary gland secretion, in milk, exist with Si Liaodengji dicalcium phosphate feed grade, tricalcium phosphate or both composite form, structure is very complicated.High as a kind of content in cow's milk, conformation is mixing protein flexibly, and casein is easily by protease hydrolysis, and its hydrolysate mainly comprises peptide, a small amount of amino acid, sugar, VITAMIN etc.These products have antibacterial disease-resistant and regulate the physiological functions such as stomach and intestine absorptions, can also promote under given conditions zooblast in-vitro multiplication, strengthen Product Expression, therefore, increasing investigator prepares the polypeptide with functional property using casein as a kind of enzymolysis substrate.As preparation have oxidation-resistance phosphopeptide caseinate, there is the polypeptide of antihypertensive function, the easy polypeptide that is absorbed by the body and promote intestinal beneficial bacterium group's growth and breeding polypeptide etc.
Northeast Agricultural University's Foodstuffs Academy Zheng Li Na and Zhang Lanwei research are found in addition, and the optimum hydrolysising condition that hydrolysis by novo casein is prepared phosphopeptide caseinate is: concentration of substrate 15%, enzyme concn 800 μ/g, pH 9.0,55 DEG C of temperature, time 2.5h.And the positive lotus hydrolysis by novo of Cai Weirong and Xue casein is prepared the optimum process condition of phosphopeptide caseinate: concentration of substrate 10%, with enzyme amount 1500 μ/g, 45 DEG C of temperature of reaction, pH10.5, reaction times 150min.These investigators all adopt Sumizyme MP and casein to prepare phosphopeptide caseinate, but the optimum preparating condition obtaining differs greatly.The zymolyte that how to obtain stable in properties under different enzymatic hydrolysis conditions seems rather important.
In industrial production, the stability of product is even more important.For a set enzymatic hydrolysis system, the principal element that affects this process has five, that is: temperature of reaction (T), concentration of substrate (S), pH, at the bottom of enzyme than (E/S), degree of hydrolysis (DH) or hydrolysis time (t).Alder-Nissen has adopted pH-stat method to control the pH of hydrolysis by novo soybean protein isolate reaction process, under lower degree of hydrolysis, measure the character of its hydrolysate, study different hydrolysising conditions as temperature, pH, ratio and the impact of concentration of substrate on hydrolysate character at the bottom of enzyme.But in industrial production, want to control completely these five hydrolysising conditions and have certain difficulty, and due to the restriction of working condition, the difference of production batch often can not ensure that each hydrolysising condition is all the same.Therefore,, under resilient working condition, the hydrolysate that obtains stabilization function and character is considerable.
At present few for the research of this aspect, the present invention wishes can be for industrial production coaches, can both obtain the enzymolysis product with stabilization function character at the bottom of different temperature-enzymes under combining.
Summary of the invention
The object of this invention is to provide a kind of preparation method that can prepare the caseic hydrolysate with stable Composition and function under different hydrolysising conditions.
Technical scheme of the present invention, taking casein as raw material, is chosen under different hydrolysising conditions and is hydrolyzed, and controls its hydrolysis, all obtains degree of hydrolysis and be 5%, 10% and 15% hydrolysate under each hydrolysising condition.Make under same degree of hydrolysis, trichoroacetic acid(TCA) (TCA) the soluble nitrogen content of the hydrolysate that different condition obtains, DPPH clearance rate does not present respectively significant difference (P<0.05), and specifically, gained Hydrolysates of Casein powder properties is stable.The steps include:
(1) preparation enzymolysis substrate: get casein, swelling with the distilled water of 10-15 times of quality, adopt the NaOH solution of 0.5M to regulate pH value to 8.5 ± 0.1, until pH value is constant, quantitative with distilled water again, making caseic final quality concentration is 4%-8%, obtains enzymolysis substrate;
(2) enzymolysis: get enzymolysis substrate prepared by step (1) and be placed in enzyme reactor, controlling temperature is 40-60 DEG C, carries out circulator bath 5min; Sumizyme MP is added in enzymolysis substrate, make enzyme-to-substrate protein mass than being 1%-3%; In enzymolysis process, be 8.5 ± 0.1 by the pH that adds alkaline solution to maintain reaction;
(3) enzyme that goes out: in the time that degree of hydrolysis reaches a fixed value in 5%-15%, the 95oC heating 10min enzyme that goes out;
(4) cooling: the hydrolyzed solution that step (3) is gone out after enzyme, through cooling, be dried and obtain yellowish or milky Hydrolysates of Casein powder.
The alkaline solution that the described alkaline solution of step (2) is 0.1M.
Gained Hydrolysates of Casein powder properties is stable, and concrete test result is as follows:
(1) otherness of the TCA soluble nitrogen content of the hydrolysate under more same degree of hydrolysis, in the time that significance level is p>0.05, otherness is not remarkable.
(2) otherness of the DPPH clearance rate of the hydrolysate under more same degree of hydrolysis, in the time that significance level is p>0.05, otherness is not remarkable.
(3) molecular weight distribution (SEC-HPLC) of the hydrolysate under more same degree of hydrolysis, be greater than 10kD, 1-10kD, 0.5-1kD and be less than the interval hydrolysate molecular weight distribution per-cent of these four of 0.5kD compared with value under reference group condition at molecular weight, deviation is in 5%, E/S=1/100, makes reference group for T=50 DEG C.
Analytical procedure:
1, pH-stat method controlled hydrolysis reaction, the method for calculating degree of hydrolysis is as follows:
In formula: the volume (mL) of B-quota of expenditure alkali;
N
bthe concentration (mol/L) of-standard base (SB);
The liberation degree of α-α amino
M
pthe content of protein (g) in-substrate;
H
totthe peptide bond sum (mmol/g) of-unit mass protein, for casein h
tot=8.2mmol/g.
2, the mensuration of nitrogen content: Micro-kjoldahl method (GB 5009
.5-1985).
3, trichoroacetic acid(TCA) (TCA) soluble nitrogen content: adopt trichloroacetic acid method to measure the solvability of hydrolysate.Concrete operation step is: take freeze-drying sample 2.0g, add 15% trichoroacetic acid(TCA) (TCA) solution 10mL, mix.Leave standstill after 5min, solution is quantitatively shifted, under 4000r/min, after centrifugal 10min, get whole supernatant liquors.Adopt Kjeldahl nitrogen determination nitrogen content, (casein protein reduction factor is 6.38).Calculation formula is as follows:
4, DPPH clearance rate: get certain density sample solution 4mL, add the DPPH solution of 1mL methyl alcohol preparation, and to make DPPH final concentration be 0.2mmol/L.Firmly jolting mixes in rearmounted darkroom and leaves standstill 30min, under 517nm, measures absorbancy.Be calculated as follows DPPH clearance rate.
In formula: A
xfor adding the absorbancy after sample solution, A
x0for the absorbancy of sample solution background, A
0for the absorbancy of blank liquid.
5, the molecular weight distribution of hydrolysate is measured.Concrete operation step is: with moving phase configuration sample solution 10mg/mL, after the cellulose acetate membrane filtration of via hole diameter 0.22 μ m, with high performance liquid chromatograph, detect by UV-detector.Configure poly saccharide peptide standard product solution simultaneously, cross sample introduction after film, make relative molecular mass calibration curve, poly saccharide peptide standard product is respectively: glycocoll-glycocoll-glycocoll (189Da), glycocoll-glycocoll-tyrosine-arginine (451Da), bacillus enzyme (1450Da), cytochrome C (12500Da).Chromatographic condition is: chromatographic column: TSKgel G2000SWXL, 300mm*7.8mm; Moving phase: Yi Jing ︰ Shui ︰ trifluoroacetic acid=45 ︰ 55 ︰ 0.1; Flow velocity: 0.5mL/min; Sample size: 20 μ L; Detect wavelength: 220nm; Column temperature: 30 DEG C, signals collecting time 30min.
Beneficial effect of the present invention: the present invention can adjust according to different working conditions, and casein hydrolysis obtains the caseic hydrolysate of same DH, makes it possess the character being equal to.The present invention can instruct industrial production, by resilient change working condition, still can ensure the stability of product.
Brief description of the drawings
The graph of molecular weight distribution of Fig. 1 casein hydrolysis degree 5%.
The graph of molecular weight distribution of Fig. 2 casein hydrolysis degree 10%.
The graph of molecular weight distribution of Fig. 3 casein hydrolysis degree 15%.
Embodiment
Below in conjunction with specific embodiment, the present invention is further described, and its specific embodiment is only construed as illustrating, and is not determinate, can not be listed as below and illustrate to limit protection scope of the present invention.
Embodiment 1
Casein substrate mass concentration is 5%, it is 50 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 1/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Under this condition, prepare degree of hydrolysis and be respectively 5%, 10% and 15% hydrolysate.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 54.36%, 64.31% and 75.34%, DPPH clearance rate be respectively 34.77%, 53.62% and 69.78%.
Embodiment 2
Casein substrate mass concentration is 5%, it is 50 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 2/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Under this condition, prepare degree of hydrolysis and be respectively 5%, 10% and 15% hydrolysate.The cooling freeze-drying of hydrolysate, obtains product.Measure DH5,10 and 15% TCA soluble nitrogen content be respectively 54.43%, 64.70% and 76.40%, DPPH clearance rate be respectively 33.88%, 54.49% and 69.48%.
Embodiment 3
Casein substrate mass concentration is 5%, it is 50 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 3/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Under this condition, prepare degree of hydrolysis and be respectively 5%, 10% and 15% hydrolysate.The cooling freeze-drying of hydrolysate, obtains product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 53.77%, 64.48% and 76.1%, DPPH clearance rate be respectively 33.89%, 54.42% and 69.15%.
Embodiment 4
Casein substrate mass concentration is 5%, it is 60 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 1/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Under this condition, prepare degree of hydrolysis and be respectively 5%, 10% and 15% hydrolysate.The cooling freeze-drying of hydrolysate, obtains product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 54.12%, 63.96% and 75.54%, DPPH clearance rate be respectively 34.60%, 54.14% and 69.67%.
Embodiment 5
Casein substrate mass concentration is 5%, it is 60 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 2/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 55.06%, 64.46% and 77.53%, DPPH clearance rate be respectively 35.01%, 54.08% and 70.10%.
Embodiment 6
Casein substrate mass concentration is 5%, it is 60 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 3/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 54.12%, 64.23% and 78.92%, DPPH clearance rate be respectively 34.57%, 54.23% and 70.47%.
Control Example 1
Casein substrate mass concentration is 5%, it is 70 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 1/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 44.97%, 63.80% and 63.13%, DPPH clearance rate be respectively 30.16%, 53.52% and 56.67%.
Control Example 2
Casein substrate mass concentration is 5%, it is 70 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 2/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 49.33%, 64.40% and 72.13%, DPPH clearance rate be respectively 37.93%, 54.03% and 64.62%.
Control Example 3
Casein substrate mass concentration is 5%, it is 70 ± 0.2 DEG C by recirculated water bath controlled hydrolysis temperature, press the ratio (E/S) 3/100 of enzyme-to-substrate albumen, add Sumizyme MP, be 8.5 ± 0.1 by the standard base (SB) control pH that adds 0.1M, reach corresponding degree of hydrolysis (DH), the 95oC heating 10min enzyme that goes out, dry, obtain zymolyte product.Measure DH5%, 10% and 15% TCA soluble nitrogen content be respectively 50.02%, 63.39% and 71.65%, DPPH clearance rate be respectively 37.62%, 54.00% and 63.34%.
Can find out from control Example 1-3, trichoroacetic acid(TCA) (TCA) the soluble nitrogen content of the hydrolysate obtaining in the time that controlled hydrolysis temperature is 70 ± 0.2 DEG C, DPPH clearance rate has significant difference (P >=0.05), and gained Hydrolysates of Casein powder properties is more unstable.
The estimation of stability of the hydrolysate of preparing under the different hydrolysising conditions of embodiment 7.
The stability of hydrolysate is whether to have significant difference than the character of the hydrolysate of the same degree of hydrolysis obtaining under combination at the bottom of investigating differing temps-enzyme.TCA soluble nitrogen content and DPPH clearance rate are done variance analysis (p<0.05) by SPSS software, the results are shown in Table 1.T=50 DEG C, the hydrolysate obtaining under E/S=1/100 condition does reference group.
Under same degree of hydrolysis, the result of the variance analysis of hydrolysate character (F-test) result black matrix band * is significant difference (p<0.05).E/S=1/100, T=50 DEG C compares group, F
0.05(1,2)=18.5, if F>18.5 illustrates under the significance level of a=0.05 have significant difference.
Table 1
The molecular weight distribution of the hydrolysate of preparing under different enzymatic hydrolysis conditions and reference group contrast, the molecular weight distribution (SEC-HPLC) of the hydrolysate of same degree of hydrolysis, be greater than 10kD, 1-10kD, 0.5-1kD and be less than the interval hydrolysate molecular weight distribution per-cent of these four of 0.5kD compared with value under reference group condition at molecular weight, deviation is in 5%.The molecular weight distribution of different DH is as shown in Fig. 1 ~ 3, and wherein as shown in Figure 1, as shown in Figure 2, the molecular weight distribution of casein hydrolysis degree 15% as shown in Figure 3 for the molecular weight distribution of casein hydrolysis degree 10% for the molecular weight distribution of casein hydrolysis degree 5%.
Claims (2)
1. utilize different hydrolysising condition preparations to there is a method for stable functional Hydrolysates of Casein, it is characterized in that step is:
(1) preparation enzymolysis substrate: get casein, swelling with the distilled water of 10-15 times of quality, adopt the NaOH solution of 0.5M to regulate pH value to 8.5 ± 0.1, until pH value is constant, quantitative with distilled water again, making caseic final quality concentration is 4%-8%, obtains enzymolysis substrate;
(2) enzymolysis: get enzymolysis substrate prepared by step (1) and be placed in enzyme reactor, controlling temperature is 40-60 DEG C, carries out circulator bath 5min; Sumizyme MP is added in enzymolysis substrate, make enzyme-to-substrate protein mass than being 1%-3%; In enzymolysis process, be 8.5 ± 0.1 by the pH that adds alkaline solution to maintain reaction;
(3) enzyme that goes out: in the time that degree of hydrolysis reaches a fixed value in 5%-15%, the 95oC heating 10min enzyme that goes out;
(4) cooling: the hydrolyzed solution that step (3) is gone out after enzyme, through cooling, be dried and obtain yellowish or milky Hydrolysates of Casein powder.
2. utilize according to claim 1 different hydrolysising condition preparations to there is the method for stable functional Hydrolysates of Casein, it is characterized in that: the alkaline solution that the described alkaline solution of step (2) is 0.1M.
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| CN106119325A (en) * | 2016-06-23 | 2016-11-16 | 哈尔滨商业大学 | A kind of preparation method with the casein hydrolysate increasing Lean mass and strength effect |
| CN108003231A (en) * | 2017-11-13 | 2018-05-08 | 江苏大学 | A kind of method of free aminoacid content in reduction small-molecular peptides |
| CN108004287A (en) * | 2017-11-13 | 2018-05-08 | 江苏大学 | A kind of preparation method of the macromolecular polypeptides based on gastro-intestinal digestion |
| CN114395601A (en) * | 2022-01-17 | 2022-04-26 | 华南理工大学 | Casein zymolyte with amphipathy and oxidation resistance and preparation method and application thereof |
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| US20120329722A1 (en) * | 2011-06-24 | 2012-12-27 | Naoto Uchida | Method for enzymatically preparing peptides for use in improvement of brain function |
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106119325A (en) * | 2016-06-23 | 2016-11-16 | 哈尔滨商业大学 | A kind of preparation method with the casein hydrolysate increasing Lean mass and strength effect |
| CN108003231A (en) * | 2017-11-13 | 2018-05-08 | 江苏大学 | A kind of method of free aminoacid content in reduction small-molecular peptides |
| CN108004287A (en) * | 2017-11-13 | 2018-05-08 | 江苏大学 | A kind of preparation method of the macromolecular polypeptides based on gastro-intestinal digestion |
| CN114395601A (en) * | 2022-01-17 | 2022-04-26 | 华南理工大学 | Casein zymolyte with amphipathy and oxidation resistance and preparation method and application thereof |
| CN114395601B (en) * | 2022-01-17 | 2023-09-29 | 华南理工大学 | Casein zymolyte with amphipathy and oxidation resistance and preparation method and application thereof |
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