CN101993476A - Casein active single peptide as well as preparation method and application thereof - Google Patents
Casein active single peptide as well as preparation method and application thereof Download PDFInfo
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- CN101993476A CN101993476A CN201010277790XA CN201010277790A CN101993476A CN 101993476 A CN101993476 A CN 101993476A CN 201010277790X A CN201010277790X A CN 201010277790XA CN 201010277790 A CN201010277790 A CN 201010277790A CN 101993476 A CN101993476 A CN 101993476A
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 37
- 239000005018 casein Substances 0.000 title claims abstract description 22
- 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 title claims abstract description 22
- 235000021240 caseins Nutrition 0.000 title claims abstract description 22
- 238000002360 preparation method Methods 0.000 title claims abstract description 9
- 235000013618 yogurt Nutrition 0.000 claims abstract description 55
- 238000000855 fermentation Methods 0.000 claims abstract description 24
- 230000004151 fermentation Effects 0.000 claims abstract description 24
- 238000000926 separation method Methods 0.000 claims abstract description 19
- 238000000746 purification Methods 0.000 claims abstract description 9
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 claims description 12
- 102000004190 Enzymes Human genes 0.000 claims description 12
- 108090000790 Enzymes Proteins 0.000 claims description 12
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 11
- 229920005654 Sephadex Polymers 0.000 claims description 9
- 239000012507 Sephadex™ Substances 0.000 claims description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical group O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 8
- 238000010521 absorption reaction Methods 0.000 claims description 8
- 239000008367 deionised water Substances 0.000 claims description 8
- 229910021641 deionized water Inorganic materials 0.000 claims description 8
- 239000012071 phase Substances 0.000 claims description 6
- 239000011347 resin Substances 0.000 claims description 6
- 229920005989 resin Polymers 0.000 claims description 6
- 238000010828 elution Methods 0.000 claims description 5
- 238000006243 chemical reaction Methods 0.000 claims description 4
- 238000010438 heat treatment Methods 0.000 claims description 4
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 4
- 239000006228 supernatant Substances 0.000 claims description 4
- 238000000108 ultra-filtration Methods 0.000 claims description 4
- 238000005227 gel permeation chromatography Methods 0.000 claims description 2
- 230000007062 hydrolysis Effects 0.000 claims description 2
- 238000006460 hydrolysis reaction Methods 0.000 claims description 2
- 230000005764 inhibitory process Effects 0.000 claims description 2
- 239000007791 liquid phase Substances 0.000 claims description 2
- 239000012528 membrane Substances 0.000 claims description 2
- 235000021262 sour milk Nutrition 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 3
- 238000005516 engineering process Methods 0.000 abstract description 3
- 238000004904 shortening Methods 0.000 abstract description 2
- 230000002401 inhibitory effect Effects 0.000 abstract 2
- 238000003277 amino acid sequence analysis Methods 0.000 abstract 1
- 238000006555 catalytic reaction Methods 0.000 abstract 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 20
- 241000894006 Bacteria Species 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- 235000014655 lactic acid Nutrition 0.000 description 10
- 239000007788 liquid Substances 0.000 description 8
- 230000004071 biological effect Effects 0.000 description 6
- 239000004310 lactic acid Substances 0.000 description 6
- 235000013336 milk Nutrition 0.000 description 6
- 239000008267 milk Substances 0.000 description 6
- 210000004080 milk Anatomy 0.000 description 6
- 239000002253 acid Substances 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 238000003860 storage Methods 0.000 description 5
- 239000000796 flavoring agent Substances 0.000 description 4
- 235000019634 flavors Nutrition 0.000 description 4
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 241001478240 Coccus Species 0.000 description 2
- 235000013960 Lactobacillus bulgaricus Nutrition 0.000 description 2
- 241000186672 Lactobacillus delbrueckii subsp. bulgaricus Species 0.000 description 2
- PVNIIMVLHYAWGP-UHFFFAOYSA-N Niacin Chemical compound OC(=O)C1=CC=CN=C1 PVNIIMVLHYAWGP-UHFFFAOYSA-N 0.000 description 2
- 241000194017 Streptococcus Species 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 2
- 229940004208 lactobacillus bulgaricus Drugs 0.000 description 2
- 235000016709 nutrition Nutrition 0.000 description 2
- 230000035764 nutrition Effects 0.000 description 2
- KJFMBFZCATUALV-UHFFFAOYSA-N phenolphthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2C(=O)O1 KJFMBFZCATUALV-UHFFFAOYSA-N 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 238000010998 test method Methods 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 241000186866 Lactobacillus thermophilus Species 0.000 description 1
- 239000005862 Whey Substances 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 235000019606 astringent taste Nutrition 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 239000012496 blank sample Substances 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 235000020247 cow milk Nutrition 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 235000015140 cultured milk Nutrition 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000005238 degreasing Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000007413 intestinal health Effects 0.000 description 1
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- 238000002156 mixing Methods 0.000 description 1
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- 235000001968 nicotinic acid Nutrition 0.000 description 1
- 229960003512 nicotinic acid Drugs 0.000 description 1
- 239000011664 nicotinic acid Substances 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 230000031068 symbiosis, encompassing mutualism through parasitism Effects 0.000 description 1
- 235000012976 tarts Nutrition 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
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Abstract
The invention provides casein active single peptide as well as a preparation method and application thereof. An amino acid sequence is Asn-Pro-Ser-Lys-Glu-Asn-Leu. In the invention, a modern catalysis technology is used for enzymolysis, a part with strong activity for prompting yogurt fermentation and inhibiting the yogurt post-acidification is separated and purified by using a biological molecule separation and purification technology, and amino acid sequence analysis is performed for the active single peptide obtained by purifying. The active peptide has the functions of obviously shortening the yogurt fermentation time and inhibiting the yogurt post-acidification, and can be safely added into the yogurt; thereby the biological active peptide is used as yogurt fermentation addictive to improve the quality of the yogurt product.
Description
Technical field
The present invention relates to the technical field that suppresses yogurt fermentation and storage, is specifically related to separate single peptide of acidifying biological activity and application thereof after the having the fermentation of the yogurt of promotion and suppressing yogurt of obtaining from casein enzymolysis liquid.
Background technology
Yogurt is meant under the effect of lactobacillus bulgaricus and thermophilus streptococcus, uses the breast that adds (or not adding) milk powder (full-cream or degreasing) to carry out lactic fermentation and the curdled milk prod that obtains, must contain a large amount of viable bacterias in the finished product.The fermentative action of milk-acid bacteria can make opalescin become fine granular curd, is easy to digest and assimilate, and milk-acid bacteria can produce the necessary VITAMIN of body nutrition, nicotinic acid and leaf in the fermenting process.Yogurt is except the whole nutrition that kept milk, and itself and the most significant difference of fresh milk are exactly the living lactic acid bacteria that is that it also contains a large amount of lactic acid and is easy to human intestinal health.
Used milk-acid bacteria mostly is the throw type leaven of buying (Direct-to vat caulture is called for short DVS) greatly abroad in China's yogurt production, and the application quantity of subculture formula yogurt bacterial classification is quite little.Compare with liquid spawn, the latent period of throw type leaven is much longer.Usually than using traditional turning over for liquid starter will prolong about 2～3 hours, for large-scale dairy plant, this is an influence factor that can not be ignored to its fermentation time.Therefore, how to shorten the fermentation time of direct-throwing bacterial classification, enhance productivity, and how to take effective means reducing the starter usage quantity, guarantee product quality simultaneously, reducing cost also is important research direction.
Thermophilus streptococcus and lactobacillus bulgaricus have growth complementary effect or are called symbiosis (Mutualism) in the yogurt fermenting process, and the growth of coccus can promote the growth of bacillus simultaneously, and the meta-bolites that the bacillus growth forms guarantees the growth of coccus.Bacterium lacticum is decomposing protein, produces acid the contribution of yogurt, and suis has vital role to the excellent flavor and the organoleptic quality of yogurt.Yogurt must keep microorganism active and good matter structure and local flavor at shelf-lives.Even refrigeration is under 0～5 ℃ of condition, the back acidifying phenomenon that the metabolism of milk-acid bacteria causes still exists, and this caused whey to separate out, tart flavour is overweight even produce astringent taste.The quality that above phenomenon has a strong impact on yogurt causes its quality guaranteed period to be shortened greatly.
Therefore, has the casein biologically active peptides that contains useful living functional factor by in yogurt, adding, promote effectively yogurt fermentation shorten fermentation time and suppress yogurt again storage period produce the back acidifying and prolong the yogurt quality guaranteed period, the yogurt industry is had great economic worth and realistic meaning.
Summary of the invention
The objective of the invention is to overcome the deficiency that prior art exists, but provide a kind of have the cow's milk source, active casein list peptide high security, that have industrialization and preparation method thereof and application.For achieving the above object, the present invention by the following technical solutions.
A kind of preparation method and application of active casein list peptide comprise the steps:
(1) at 50 ℃～55 ℃, add papoid under the condition of pH 6.0-7.5 casein is carried out enzymolysis, get enzymolysis solution;
(2) when degree of hydrolysis reaches 9%～10%, 90～95 ℃ of heating 15～20min enzymes that go out, enzymolysis reaction is with the molecular weight of control biologically active peptides;
(3) enzymolysis solution that enzyme lives that will go out carries out separation and purification by membrane sepn, macroporous resin, gel chromatography, reversed phase high efficiency liquid phase successively, promptly gets described biologically active peptides.
Above-mentioned preparation method, the enzymolysis solution that the enzyme that will go out in the step (3) is lived under 4 ℃ centrifugal 20 minutes with 6000 g, with supernatant liquor after ultrafiltration (getting molecular weight) less than 3000 daltonian components, adopt macroporous resin NKA-II, collect 10-20%(w/w) ethanol eluate, then adopt the Sephadex(dextrane gel) G-25, moving phase is deionized water, detect wavelength 220nm, press the absorption peak order and collect; Has stronger active component again through C through what Sephadex G-25 separation obtained
18The high performance liquid chromatography separation and purification, separation condition is: 5-40% acetonitrile and 95-60% deionized water gradient elution, detect wavelength 220nm, press the absorption peak order and collect.
Acidifying active casein list peptide after the present invention also provides and promoted the yogurt fermentation and suppressed yogurt by having of making of above-mentioned preparation method.
Above-mentioned active casein list peptide, measuring its molecular weight by liquid chromatography-esi-msn is 801.4 dalton, this active peptide aminoacid sequence is shown in sequence in the sequence table 1.
Described active casein list peptide can be applicable to promote Yoghourt fermentation in the yogurt fermentation, acidifying after the inhibition sour milk.
The present invention has adopted above technical scheme, has following advantage and effect:
1, to have obtained aminoacid sequence by further separation, purifying to casein enzymolysis liquid be the peptide of NPSKENL in the present invention, acidification after this bioactive peptide has obvious shortening yogurt fermentation time and suppresses yogurt.
2, the biologically active peptides of separation and purification gained of the present invention is to separate the newborn source property peptide obtain from casein, interpolation that can safety in yogurt.
Description of drawings
Fig. 1 is the initial gross separation figure of Sephadex G-25 to casein enzymolysis liquid;
Fig. 2 is the separation and purification figure of RP-HPLC to biologically active peptides;
Fig. 3 is for adding 50ppm(w/w in the embodiment) the single peptide of biological activity is to the yogurt fermentation period and the influence curve in blank relative acid milk fermentation cycle;
Fig. 4 is for adding 50ppm(w/w in the embodiment) the single peptide of biological activity produces the influence curve of acid and the influence curve of blank correspondence to the yogurt shelf lives.
Fig. 5 is for adding 50ppm(w/w in the embodiment) the single peptide of biological activity to the influence curve of yogurt shelf lives viable lactic acid bacteria number and the influence curve of blank correspondence.
Specific embodiments
Below in conjunction with drawings and Examples concrete enforcement of the present invention is described further.
Embodiment 1: utilize the production of casein enzymolysis liquid to have the fermentation of significant promotion yogurt and suppress yogurt after the single peptide of acidifying biological activity
1, Controlled-enzymatic Hydrolysis: at 50 ℃, add papoid under the condition of pH 6.0 casein is carried out enzymolysis, get enzymolysis solution.
2, the enzymolysis solution enzyme that goes out: 90 ℃ of heating 15min enzyme that goes out, enzymolysis reaction.
3, the enzymolysis solution centrifugal (6000 x g, 4 ℃) 20 minutes that enzyme lives that will go out, (it is little to get molecular weight through ultrafiltration with supernatant liquor
In 3000 daltonian components) after, adopt macroporous resin NKA-II, collect 10%(w/w) ethanol eluate, then adopting Sephadex G-25, moving phase is deionized water, detects wavelength 220nm, presses the absorption peak order and collects, as shown in Figure 1.Has stronger active component again through C through what Sephadex G-25 separation obtained
18The high performance liquid chromatography separation and purification, separation condition is: 5%(w/w) acetonitrile and 95%(w/w) the deionized water gradient elution, detect wavelength 220nm, press the absorption peak order and collect, as shown in Figure 2.
Embodiment 2: utilize the production of casein enzymolysis liquid to have the fermentation of significant promotion yogurt and suppress yogurt after the single peptide of acidifying biological activity
1, Controlled-enzymatic Hydrolysis: at 55 ℃, add papoid under the condition of pH 7.5 casein is carried out enzymolysis, get enzymolysis solution.
2, the enzymolysis solution enzyme that goes out: 95 ℃ of heating 20min enzyme that goes out, enzymolysis reaction.
3, the enzymolysis solution centrifugal (6000 x g, 4 ℃) 20 minutes that enzyme lives that will go out, (it is little to get molecular weight through ultrafiltration with supernatant liquor
In 3000 daltonian components) after, adopt macroporous resin NKA-II, collect 20%(w/w) ethanol eluate, then adopting Sephadex G-25, moving phase is deionized water, detects wavelength 220nm, presses the absorption peak order and collects, as shown in Figure 1.Has stronger active component again through C through what Sephadex G-25 separation obtained
18The high performance liquid chromatography separation and purification, separation condition is: 40%(w/w) acetonitrile and 60%(w/w) the deionized water gradient elution, detect wavelength 220nm, press the absorption peak order and collect, as shown in Figure 2.
Embodiment 3: biologically active peptides is to the influence of yogurt fermentation period
Before yogurt fermentation, add 50ppm(w/w) proteic milk powder such as embodiment 1 gained biologically active peptides HAQQKE replacement, mensuration yogurt fermentation period, i.e. T
PH4.5, yogurt fermented to the needed time of pH4.5, and unit is hour.As shown in Figure 3, the yogurt fermentation period has shortened 23.00% behind the interpolation NPSKENL.
Embodiment 3: biologically active peptides is to the influence of the acidity variation of yogurt shelf time
Mensuration is clean Neil degree T by 2 fermented yogurts of embodiment at the titration acidity of 28 days storage periods
0Change.
Test method: get the fermented-milk 5ml that stirs with the 5ml suction pipe, adding contains in the 25ml distilled water Erlenmeyer flask, splashes into 3～4 1% phenolphthalein indicators, to light red, keeps 20s not fade with the 0.1NNaOH titration.The milliliter number that consumes NaOH solution multiply by 20 and is acidity T
0
As seen from Figure 4, produce the acid amount after yogurt stores 28 days behind the interpolation NPSKENL and reduced 24.07% with respect to blank sample, this shows that the NPSKENL of 50ppm can obviously suppress to produce acid in the newborn storage process of yogurt, helps to keep the yogurt product special flavour, extends the shelf life.
Embodiment 4: biologically active peptides is to the influence of the viable lactic acid bacteria number variation of yogurt shelf time
Measure and press of the viable lactic acid bacteria number variation of 2 fermented yogurts of embodiment, adopt test tube method at 28 days storage periods.
Test method: under aseptic technique, yogurt is stirred, pipettes 1ml, add and to contain the 9ml diluent in vitro, make the even diluent of 1 ﹕ 10, and on the eddy current instrument abundant mixing.From the latter, draw 1ml again in the 9ml diluent, and take turns doing 10 times and increase progressively and be diluted to 10
-6, 10
-7Two extent of dilution.Each extent of dilution is drawn 1ml in sterilization test tube substratum, makees two parallel samples, cultivates 72h in 37 ℃ of constant incubators.
Fig. 5 shows that behind the interpolation NPSKENL, yogurt viable lactic acid bacteria number after storing 28 days is 2.35 times of barren, and the result shows that life bioactive peptide NPSKENL can significantly promote the lactobacter growth breeding, improves the yogurt quality.
Claims (4)
1. active casein list peptide, this active peptide aminoacid sequence is shown in sequence in the sequence table 1.
2. the preparation method of the described a kind of active casein list peptide of claim 1 is characterized in that comprising the steps:
(1) at 50 ℃～55 ℃, add papoid under the condition of pH 6.0-7.5 casein is carried out enzymolysis, get enzymolysis solution;
(2) when degree of hydrolysis reaches 9%～10%, 90～95 ℃ of heating 15～20min enzymes that go out, enzymolysis reaction is with the molecular weight of control biologically active peptides;
(3) enzymolysis solution that enzyme lives that will go out carries out separation and purification by membrane sepn, macroporous resin, gel chromatography, reversed phase high efficiency liquid phase successively, promptly gets described biologically active peptides.
3. preparation method according to claim 2, the enzymolysis solution that the enzyme that it is characterized in that will going out in the step (3) is lived under 4 ℃ centrifugal 20 minutes with 6000 g, supernatant liquor through ultrafiltration, is got molecular weight less than 3000 daltonian components, adopt macroporous resin NKA-II, use 10-20%(w/w) ethanol elution, collect elutriant, then adopt Sephadex G-25, moving phase is deionized water, detect wavelength 220nm, press the absorption peak order and collect; Has stronger active component again through C through what Sephadex G-25 separation obtained
18The high performance liquid chromatography separation and purification, separation condition is: 5-40% acetonitrile and 95-60% deionized water gradient elution, detect wavelength 220nm, press the absorption peak order and collect.
4. the described active casein list of claim 1 peptide is applied to promote Yoghourt fermentation in the yogurt fermentation, acidifying after the inhibition sour milk.
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102352398A (en) * | 2011-09-30 | 2012-02-15 | 华南理工大学 | Casein active single peptide as well as preparation method and application thereof |
| CN102771557A (en) * | 2012-08-10 | 2012-11-14 | 光明乳业股份有限公司 | Beverage containing functional hydrolyzed protein peptide milk and preparation method thereof |
| CN102861315A (en) * | 2012-10-19 | 2013-01-09 | 广东海洋大学 | Preparation method of casein anticoagulant peptide oral liquid |
| CN108623669A (en) * | 2018-05-02 | 2018-10-09 | 扬州大学 | Immune-active peptides and its enrichment method and application in a kind of acidified milk |
| WO2021246392A1 (en) * | 2020-06-02 | 2021-12-09 | アサヒグループホールディングス株式会社 | Lactic acid bacteria growth promoter |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101580861A (en) * | 2009-06-05 | 2009-11-18 | 华南理工大学 | Biologically active peptide capable of inhibiting after-fermentation of acidified milk and preparation method thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN101580861A (en) * | 2009-06-05 | 2009-11-18 | 华南理工大学 | Biologically active peptide capable of inhibiting after-fermentation of acidified milk and preparation method thereof |
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| 徐成勇等: "弱后酸化酸奶发酵剂的筛选", 《中国乳品工业》 * |
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Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102352398A (en) * | 2011-09-30 | 2012-02-15 | 华南理工大学 | Casein active single peptide as well as preparation method and application thereof |
| CN102352398B (en) * | 2011-09-30 | 2015-07-01 | 华南理工大学 | Casein active single peptide as well as preparation method and application thereof |
| CN102771557A (en) * | 2012-08-10 | 2012-11-14 | 光明乳业股份有限公司 | Beverage containing functional hydrolyzed protein peptide milk and preparation method thereof |
| CN102861315A (en) * | 2012-10-19 | 2013-01-09 | 广东海洋大学 | Preparation method of casein anticoagulant peptide oral liquid |
| CN108623669A (en) * | 2018-05-02 | 2018-10-09 | 扬州大学 | Immune-active peptides and its enrichment method and application in a kind of acidified milk |
| CN108623669B (en) * | 2018-05-02 | 2021-07-09 | 扬州大学 | Immune active peptide in fermented milk and enrichment method and application thereof |
| WO2021246392A1 (en) * | 2020-06-02 | 2021-12-09 | アサヒグループホールディングス株式会社 | Lactic acid bacteria growth promoter |
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