CN105734103B - The preparation method of casein hydrolysate peptides - Google Patents
The preparation method of casein hydrolysate peptides Download PDFInfo
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- CN105734103B CN105734103B CN201610309219.9A CN201610309219A CN105734103B CN 105734103 B CN105734103 B CN 105734103B CN 201610309219 A CN201610309219 A CN 201610309219A CN 105734103 B CN105734103 B CN 105734103B
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 36
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 24
- 108010079058 casein hydrolysate Proteins 0.000 title claims abstract description 22
- 238000002360 preparation method Methods 0.000 title claims abstract description 22
- 108090000790 Enzymes Proteins 0.000 claims abstract description 44
- 102000004190 Enzymes Human genes 0.000 claims abstract description 44
- 108010076119 Caseins Proteins 0.000 claims abstract description 30
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 claims abstract description 30
- 235000021240 caseins Nutrition 0.000 claims abstract description 30
- 239000005018 casein Substances 0.000 claims abstract description 29
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 16
- 239000007788 liquid Substances 0.000 claims abstract description 11
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 5
- 230000009849 deactivation Effects 0.000 claims abstract description 4
- 238000001556 precipitation Methods 0.000 claims abstract description 4
- 238000004090 dissolution Methods 0.000 claims abstract description 3
- 238000004108 freeze drying Methods 0.000 claims abstract description 3
- 229940088598 enzyme Drugs 0.000 claims description 41
- 239000004365 Protease Substances 0.000 claims description 32
- SERLAGPUMNYUCK-DCUALPFSSA-N 1-O-alpha-D-glucopyranosyl-D-mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O SERLAGPUMNYUCK-DCUALPFSSA-N 0.000 claims description 16
- 108010004032 Bromelains Proteins 0.000 claims description 15
- 108090000526 Papain Proteins 0.000 claims description 15
- 235000019835 bromelain Nutrition 0.000 claims description 15
- RQFQJYYMBWVMQG-IXDPLRRUSA-N chitotriose Chemical compound O[C@@H]1[C@@H](N)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](N)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)N)[C@@H](CO)O1 RQFQJYYMBWVMQG-IXDPLRRUSA-N 0.000 claims description 15
- 235000010439 isomalt Nutrition 0.000 claims description 15
- 239000000905 isomalt Substances 0.000 claims description 15
- HPIGCVXMBGOWTF-UHFFFAOYSA-N isomaltol Natural products CC(=O)C=1OC=CC=1O HPIGCVXMBGOWTF-UHFFFAOYSA-N 0.000 claims description 15
- 235000019834 papain Nutrition 0.000 claims description 15
- 229940055729 papain Drugs 0.000 claims description 15
- -1 trypsase Proteins 0.000 claims description 7
- 239000012528 membrane Substances 0.000 claims description 3
- 238000000926 separation method Methods 0.000 claims description 2
- 230000014759 maintenance of location Effects 0.000 claims 1
- 230000007062 hydrolysis Effects 0.000 abstract description 9
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 9
- 239000000047 product Substances 0.000 abstract description 8
- 239000002994 raw material Substances 0.000 abstract description 5
- 150000001413 amino acids Chemical class 0.000 abstract description 4
- 239000000126 substance Substances 0.000 abstract description 4
- 238000010521 absorption reaction Methods 0.000 abstract description 3
- 230000006870 function Effects 0.000 abstract description 3
- 102000015636 Oligopeptides Human genes 0.000 abstract description 2
- 108010038807 Oligopeptides Proteins 0.000 abstract description 2
- 206010070834 Sensitisation Diseases 0.000 abstract description 2
- 230000003712 anti-aging effect Effects 0.000 abstract description 2
- 230000010261 cell growth Effects 0.000 abstract description 2
- 238000003912 environmental pollution Methods 0.000 abstract description 2
- 230000036039 immunity Effects 0.000 abstract description 2
- 239000006210 lotion Substances 0.000 abstract description 2
- 230000008313 sensitization Effects 0.000 abstract description 2
- 102000011632 Caseins Human genes 0.000 description 22
- 238000012360 testing method Methods 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 238000013329 compounding Methods 0.000 description 5
- 235000018102 proteins Nutrition 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 3
- 239000013566 allergen Substances 0.000 description 3
- 230000000845 anti-microbial effect Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 230000035790 physiological processes and functions Effects 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 235000019419 proteases Nutrition 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000010189 synthetic method Methods 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 230000002785 anti-thrombosis Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 229940021722 caseins Drugs 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000012009 microbiological test Methods 0.000 description 1
- 239000002366 mineral element Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
Classifications
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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
-
- 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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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Water Supply & Treatment (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
The invention discloses a kind of preparation methods of casein hydrolysate peptides, comprising the following steps: (1) dissolution of casein water is configured to the casein solution that mass concentration is 5-15wt%, and adjusts pH to 5-10；(2) enzyme and enzyme live keeping agent are added in casein solution, are hydrolyzed 1-5 hours at 45-75 DEG C；(3) enzyme deactivation is 5-15 minutes living under 85-100 DEG C of water-bath, obtains enzymolysis liquid；(4) pH value of enzymolysis liquid is adjusted to 4-5 isoelectric precipitation, is centrifugated；(5) ultrafiltration, freeze-drying.The preparation method of casein hydrolysate peptides of the present invention, degree of hydrolysis is moderate, and oligopeptides content is high, and free amino acid is low, and sensitization is low, absorption easy to digest.Unharmful substance in raw material used in the present invention, it is free from environmental pollution, and also raw material sources of the present invention are extensive, and preparation process is simple, and product has the function of improving immunity, beautifying face and moistering lotion, promotes cell growth, anti-aging.
Description
Technical field
The present invention relates to technical field of health care food, and in particular to a kind of preparation method of casein hydrolysate peptides.
Background technique
The study found that the mankind ingest, protein is in the form of small peptide mostly after gastral enzyme effect to modern nutriology
Digest and assimilate, another new knowledge of peptide trophism be protein can produce in enzymolysis process it is some have special physiological tune
Save the biologically active peptide of function.
Casein (casein) is a kind of protein rich in bioactive sequences, in specific restriction endonuclease (such as tryptose
Enzyme etc.) and similar under physiological condition, these bioactive sequences can be released, and obtain biologically active casein biology
Active peptide.These biologically active peptides are adjusting gastrointestinal movement, adjusting immune system, the raising of anti-blood pressure, antibacterial, antithrombotic, are resisting
Virus, anticancer, removing free radical and promotion mineral element absorption etc. play an important role.
At present there are mainly three types of the preparation methods of biologically active peptide: (1) extraction method is extracted from the organism of nature
Itself intrinsic natural activity peptide；(2) Hydrolyze method protein is hydrolyzed to obtain and have the biology of physiological function living
Property peptide；(3) synthetic method, i.e. applied chemistry synthetic method prepare biologically active peptide.It is selected based on different purposes different
Preparation method, different preparation methods respectively have advantage and disadvantage.
Protein inherently bioactivity propeptide, selects these polypeptide chains of suitable protease hydrolytic, having
The peptide fragment of bioactivity releases, so as to prepare the biologically active peptide with physiological function.Using Production by Enzymes activity
Peptide is the hot spot of current research.Enzymatic hydrolysis has the advantages that many physics, chemical modification are incomparable.First it be it is a kind of not
Completely, halfway hydrolysis, product are mainly peptide rather than amino acid；The mild condition followed by reacted, the reaction time is short,
It is high-efficient, racemization is not generated, amino acid is not also destroyed；It is product purity height again, product is easily separated, low in cost etc. excellent
Point；In addition, using protease come aminosal when, the type of selection enzyme can also be passed through, the measures of control reaction condition etc. come
Obtain the biologically active peptide with particular physiological function.
The present invention provides a kind of preparation method of casein hydrolysate peptides, it is easy to absorb, and casein can be effectively reduced
The content of middle anaphylactogen.
Summary of the invention
In view of the deficiencies of the prior art, technical problem to be solved by the invention is to provide a kind of systems of casein hydrolysate peptides
Preparation Method.
To achieve the above object, the adopted technical solution is that:
A kind of preparation method of casein hydrolysate peptides, comprising the following steps:
(1) dissolution of casein water is configured to the casein solution that mass concentration is 5-15wt%, and adjusts pH to 5-
10；
(2) enzyme and enzyme live keeping agent are added in casein solution, are hydrolyzed 1-5 hours at 45-75 DEG C；
(3) enzyme deactivation is 5-15 minutes living under 85-100 DEG C of water-bath, obtains enzymolysis liquid；
(4) pH value of enzymolysis liquid is adjusted to 4-5 isoelectric precipitation, is centrifugated；
(5) ultrafiltration, freeze-drying.
PH value is adjusted in the step (1) and step (4) can be using NaOH solution, HCl solution etc..
Preferably, in the step (2) enzyme additional amount be casein solution quality 0.5-5%, enzyme live keeping agent plus
Enter the 0.1-1% that amount is casein solution quality.
Preferably, the enzyme in the step (2) be papain, trypsase, it is one or more in bromelain
Mixture.
It is highly preferred that the enzyme in the step (2) is mixed by papain, trypsase, bromelain, institute
State papain, trypsase, bromelain mass ratio be (1-3): (1-3): (1-3).
Preferably, the enzyme live keeping agent in the step (2) is six sugar of shell, isomalt, one kind or more in chitotriose
The mixture of kind.
It is highly preferred that the enzyme live keeping agent in the step (2) is mixed by six sugar of shell, isomalt, chitotriose,
Six sugar of shell, isomalt, chitotriose mass ratio be (1-3): (1-3): (1-3).
Preferably, the centrifuge separation revolving speed in the step (4) is 2000-5000 revs/min, and the time is 20-40 minutes.
Preferably, the ultrafiltration in the step (5) is the ultrafiltration membrane ultrafiltration with molecular cut off 1-10kD.
The preparation method of casein hydrolysate peptides of the present invention, degree of hydrolysis is moderate, and oligopeptides content is high, and free amino acid is low, sensitization
Low, the absorption easy to digest of property.Unharmful substance in raw material used in the present invention, it is free from environmental pollution, and raw material sources of the present invention
Extensively, preparation process is simple, and product has the function of improving immunity, beautifying face and moistering lotion, promotes cell growth, anti-aging.
Specific embodiment
The present invention will be further explained with reference to the examples below, as described below, is only to preferable implementation of the invention
Example, not limits the present invention, any person skilled in the art is possibly also with the disclosure above
Technology contents be changed to the equivalent embodiment changed on an equal basis.Without departing from the concept of the present invention, according to the present invention
Technical spirit any simple modification or equivalent variations that following embodiment is made, fall within the scope of protection of the present invention.
Each raw material introduction in embodiment:
Six sugar of shell, No. CAS: 41708-95-6.
Isomalt, No. CAS: 64519-82-0.
Chitotriose, No. CAS: 41708-93-4.
Papain, No. CAS: 9001-73-4, Zhengzhou Kang Yuan chemical products Co., Ltd provides, enzyme activity 200U/mg.
Trypsase, No. CAS: 9002-07-7, the good fraternal chemical products Co., Ltd in Zhengzhou provides, enzyme activity 200U/mg.
Bromelain, No. CAS: 9001-00-7, Shandong Sheng Xie Biotechnology Co., Ltd provides, enzyme activity 200U/mg.
Embodiment 1
The preparation method of casein hydrolysate peptides, comprising the following steps:
(1) that casein is configured to the casein solution that mass concentration is 10wt% with deionized water dissolving is (100 grams i.e. every
10 grams of caseins of deionized water dissolving), and pH to 7.8 is adjusted with the sodium hydroxide solution of 2mol/L；
(2) enzyme and enzyme live keeping agent are added in casein solution and are uniformly mixed, wherein the additional amount of enzyme is casein
The 1.2% of solution quality, the additional amount of enzyme live keeping agent be casein solution quality 0.6% (i.e. every 100 grams of casein solutions add
Enter 1.2 grams of enzyme, 0.6 gram of enzyme live keeping agent), it is hydrolyzed 2 hours at 60 DEG C, product after being hydrolyzed；
(3) product after hydrolysis is then placed in the lower enzyme deactivation in 10 minutes of 95 DEG C of water-baths to live, obtains enzymolysis liquid；
(4) pH value of enzymolysis liquid is adjusted with the hydrochloric acid solution of 2mol/L to 4.6 casein isoelectric points, after precipitation to be precipitated,
Unhydrolysed casein is removed with 3000r/min speed centrifugation 30min, the supernatant after being centrifuged；
(5) the ultrafiltration membrane ultrafiltration of the supernatant molecular cut off 6kD after taking centrifugation is collected filtrate, is frozen at -30 DEG C
It is dry, obtain the casein hydrolysate peptides of the preparation of embodiment 1.
Enzyme in the step (2) is 1:1:1 stirring by papain, trypsase, bromelain in mass ratio
It is uniformly mixed and obtains.
Enzyme live keeping agent in the step (2) is stirred in mass ratio for 1:1:1 by six sugar of shell, isomalt, chitotriose
It mixes to be uniformly mixed and obtain.
Embodiment 2
Substantially the same manner as Example 1, difference is only in that: the enzyme by papain, trypsase in mass ratio
It is uniformly mixed to obtain for 1:1.It can be prepared by the casein hydrolysate peptides of embodiment 2.
Embodiment 3
Substantially the same manner as Example 1, difference is only in that: the enzyme is by papain, bromelain by quality
Than being uniformly mixed to obtain for 1:1.It can be prepared by the casein hydrolysate peptides of embodiment 3.
Embodiment 4
Substantially the same manner as Example 1, difference is only in that: the enzyme by trypsase, bromelain in mass ratio
It is uniformly mixed to obtain for 1:1.It can be prepared by the casein hydrolysate peptides of embodiment 4.
Embodiment 5
Substantially the same manner as Example 1, difference is only in that: the enzyme live keeping agent is pressed by six sugar of shell, isomalt
Mass ratio is that 1:1 is uniformly mixed to obtain.It can be prepared by the casein hydrolysate peptides of embodiment 5.
Embodiment 6
Substantially the same manner as Example 1, difference is only in that: the enzyme live keeping agent by the sugar of shell six, chitotriose in mass ratio
It is uniformly mixed to obtain for 1:1.It can be prepared by the casein hydrolysate peptides of embodiment 6.
Embodiment 7
Substantially the same manner as Example 1, difference is only in that: the enzyme live keeping agent is pressed by isomalt, chitotriose
Mass ratio is that 1:1 is uniformly mixed to obtain.It can be prepared by the casein hydrolysate peptides of embodiment 7.
Test case 1
The enzymolysis liquid obtained to embodiment 1-7 step (3) tests its degree of hydrolysis, and concrete outcome is shown in Table 1:
Table 1: casein hydrolysis degree tests table
| Degree of hydrolysis/% | |
| Embodiment 1 | 17.60 |
| Embodiment 2 | 8.30 |
| Embodiment 3 | 8.76 |
| Embodiment 4 | 9.89 |
| Embodiment 5 | 8.18 |
| Embodiment 6 | 7.65 |
| Embodiment 7 | 8.12 |
Comparing embodiment 1 and embodiment 2-4, embodiment 1 (papain, trypsase, bromelain) degree of hydrolysis
It is apparently higher than embodiment 2-4 (papain, trypsase, any two kinds of compoundings in bromelain).Comparing embodiment 1 with
Embodiment 5-7, embodiment 1 (six sugar of shell, isomalt, chitotriose) degree of hydrolysis be apparently higher than embodiment 2-4 (sugar of shell six,
Any two kinds of compoundings in isomalt, chitotriose).
Test case 2
The enzymolysis liquid of the casein solution of embodiment 1-7 step (1) preparation and step (3) preparation is subjected to allergen content
Test, is calculated anaphylactogen reduced rate, calculation formula are as follows: and anaphylactogen reduced rate (%)=(anaphylactogen contains in casein solution
Allergen content in amount-enzymolysis liquid) allergen content × 100% in/casein solution, concrete outcome is shown in Table 2.
Table 2: anaphylactogen reduced rate
| Anaphylactogen reduced rate/% | |
| Embodiment 1 | 99.92 |
| Embodiment 2 | 93.03 |
| Embodiment 3 | 93.32 |
| Embodiment 4 | 94.45 |
| Embodiment 5 | 92.67 |
| Embodiment 6 | 92.83 |
| Embodiment 7 | 93.89 |
Comparing embodiment 1 and embodiment 2-4, embodiment 1 (papain, trypsase, bromelain) anaphylactogen
Reduced rate is apparently higher than embodiment 2-4 (papain, trypsase, any two kinds of compoundings in bromelain).Compare reality
Example 1 and embodiment 5-7 are applied, embodiment 1 (six sugar of shell, isomalt, chitotriose) anaphylactogen reduced rate is apparently higher than implementation
Example 2-4 (six sugar of shell, isomalt, in chitotriose any two kinds compound).
Test case 3
Casein hydrolysate peptides prepared by embodiment 1-7 are placed in 25 DEG C, preservation half a year under 85% environment of relative humidity, adopt
Total plate count test is carried out with " measurement of GB/T 4789.2-2010 microbiological test of food hygiene total plate count ".Specific test
It the results are shown in Table 3.
Table 3: total plate count tests table cfu/g
| Total plate count | |
| Embodiment 1 | 1.6×103 |
| Embodiment 2 | 3.2×103 |
| Embodiment 3 | 4.1×103 |
| Embodiment 4 | 3.5×103 |
| Embodiment 5 | 4.3×103 |
| Embodiment 6 | 4.7×103 |
| Embodiment 7 | 4.5×103 |
Inventor is found surprisingly that after addition enzyme and enzyme live keeping agent, total plate count is decreased obviously, the anti-microbial property of product
It significantly improves, the shelf-life is substantially extended.Comparing embodiment 1 and embodiment 2-4, embodiment 1 (papain, tryptose
Enzyme, bromelain) to be apparently higher than embodiment 2-4 (papain, trypsase, any in bromelain for anti-microbial property
Two kinds of compoundings).Comparing embodiment 1 and embodiment 5-7, embodiment 1 (six sugar of shell, isomalt, chitotriose) anti-microbial property
It is apparently higher than embodiment 2-4 (six sugar of shell, isomalt, any two kinds of compoundings in chitotriose).
Claims (4)
1. a kind of preparation method of casein hydrolysate peptides, which comprises the following steps:
(1) dissolution of casein water is configured to the casein solution that mass concentration is 5-15wt%, and adjusts pH to 5-10；
(2) enzyme and enzyme live keeping agent are added in casein solution, are hydrolyzed 1-5 hours at 45-75 DEG C；The enzyme live keeping agent
Mixed by six sugar of shell, isomalt, chitotriose, six sugar of shell, isomalt, chitotriose mass ratio be
1-3: 1-3: 1-3；
(3) enzyme deactivation is 5-15 minutes living under 85-100 DEG C of water-bath, obtains enzymolysis liquid；
(4) pH value of enzymolysis liquid is adjusted to 4-5 isoelectric precipitation, is centrifugated；
(5) ultrafiltration, freeze-drying；
The enzyme is mixed by papain, trypsase, bromelain, the papain, trypsase,
The mass ratio of bromelain is 1-3: 1-3: 1-3.
2. the preparation method of casein hydrolysate peptides as described in claim 1, it is characterised in that: the centrifuge separation revolving speed is
2000-5000 revs/min, the time is 20-40 minutes.
3. the preparation method of casein hydrolysate peptides as described in claim 1, it is characterised in that: the ultrafiltration is with retention point
The ultrafiltration membrane ultrafiltration of son amount 1-10kD.
4. the preparation method of casein hydrolysate peptides as described in claim 1, it is characterised in that: enzyme in the step (2)
Additional amount is 0 .5-5% of casein solution quality, and the additional amount of enzyme live keeping agent is 0 .1-1% of casein solution quality.
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Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101748170A (en) * | 2010-01-22 | 2010-06-23 | 西北大学 | Method for preparing 1-deoxy-D-xylulose with chemical method-enzymatic method |
| CN102250998A (en) * | 2011-05-27 | 2011-11-23 | 山东省花生研究所 | Preparation method for peanut bioactive peptide |
| CN104059127A (en) * | 2014-05-29 | 2014-09-24 | 无限极（中国）有限公司 | Natural high-activity antihypertensive peptide, and preparation method and application thereof |
| CN105077261A (en) * | 2015-09-24 | 2015-11-25 | 上海韬鸿化工科技有限公司 | Composite fruit and vegetable ferment and preparing method thereof |
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2016
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Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101748170A (en) * | 2010-01-22 | 2010-06-23 | 西北大学 | Method for preparing 1-deoxy-D-xylulose with chemical method-enzymatic method |
| CN102250998A (en) * | 2011-05-27 | 2011-11-23 | 山东省花生研究所 | Preparation method for peanut bioactive peptide |
| CN104059127A (en) * | 2014-05-29 | 2014-09-24 | 无限极（中国）有限公司 | Natural high-activity antihypertensive peptide, and preparation method and application thereof |
| CN105077261A (en) * | 2015-09-24 | 2015-11-25 | 上海韬鸿化工科技有限公司 | Composite fruit and vegetable ferment and preparing method thereof |
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