CN102746395A - Method for separating beta-lactoglobulin from raw milk - Google Patents
Method for separating beta-lactoglobulin from raw milk Download PDFInfo
- Publication number
- CN102746395A CN102746395A CN2012102317977A CN201210231797A CN102746395A CN 102746395 A CN102746395 A CN 102746395A CN 2012102317977 A CN2012102317977 A CN 2012102317977A CN 201210231797 A CN201210231797 A CN 201210231797A CN 102746395 A CN102746395 A CN 102746395A
- Authority
- CN
- China
- Prior art keywords
- beta
- filtrating
- centrifugal
- under
- oglobulin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
Images
Landscapes
- Peptides Or Proteins (AREA)
- Dairy Products (AREA)
Abstract
The invention discloses a method for separating beta-lactoglobulin from raw milk. The method comprises the following steps: with fresh cow's milk as a processing object, carrying out centrifugation and degreasing so as to obtain skim milk; adding an acid to adjust the pH value of the skim milk, standing the skim milk for a certain period of time and then removing casein through centrifugation; adjusting the pH value of a solution so as to allow the solution to be acidic, adding a salt, standing the solution for a certain period of time, then carrying out centrifugation and collecting supernatant; adjusting the pH value of the supernatant, adding a sodium salt, carrying out centrifugation after standing and collecting precipitate; flushing the precipitate and then dissolving the precipitate in a PBS buffer solution; carrying out ultrafiltration on the solution to remove salt and carrying out freeze-drying; and identifying beta-lactoglobulin by using sodium dodecanesulphonate-polyacrylamide gel electrophoresis and quantifying purity by using reverse-phase chromatography. According to the method provided in the invention, beta-lactoglobulin can be separated from fresh cow's milk through acid deposition and salt precipitation, and desalting through ultrafiltration is combinedly used so as to obtain high purity beta-lactoglobulin. The method improves separation efficiency of beta-lactoglobulin and provides a high-quality raw material for research on other aspects of and application of beta-lactoglobulin.
Description
Technical field
What the present invention relates to is a kind of separation purification method of beta-lact oglobulin, specifically a kind of from fresh milk the method for high efficiency separation and purifying beta-lact oglobulin.
Background technology
Beta-lact oglobulin is present in most of mammiferous Ruzhongs, is that concentration is about 3.2g/L in cow's milk, mainly exists with dimeric form by the peculiar albumen of mammary epithelial cell synthetic breast, and 2 monomers are connected by non covalent bond.When pH＜3.0 or pH＞7.0, the beta-lact oglobulin dimer is dissociated into monomer.Monomer beta-lact oglobulin molecular weight is about 18300 dalton, and iso-electric point is 5.1～5.3.Beta-lact oglobulin accounts for about 55% of whey-protein, is the major protein in the whey, is the function embodiment person of whey-protein.It has processing characteristics such as BA and good whipping whipability, gelation, film-forming properties such as changing the cow's milk thermostability, combine with lipid acid and flavour substances, be anticancer, is widely used in food-processing, makeup, medicine and other fields.Existing at present method of separating beta-lact oglobulin, for example affinity chromatography, preparative hplc, dialysis etc., but treatment capacity is less, and instrument is complicated, preparation cost is high.
Summary of the invention
The technical problem that the present invention will solve provides that a kind of preparation is simple and easy, purity is high, the beta-lact oglobulin that cost is low.
In order to solve the problems of the technologies described above, the present invention provides a kind of method of from raw dairy, separating beta-lact oglobulin, comprises the steps:
1), with fresh milk in 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, thereby remove dairy fats, filtrating first;
2), filtrating is regulated pH to 4.5 ~ 4.7 first, leaves standstill 20 ~ 40min under the room temperature; Filtrate first after must handling;
3), filtrate first after will handling in 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, the filtrating of gained is repeated centrifugal and the absorbent gauze filtration treatment above-mentioned 3 ~ 5 ℃ under, must filtrate by secondary;
4), secondary filtrating is regulated pH to 1.9 ~ 2.1, secondary filtrating after must handling;
5), handle back secondary filtrating according to every 1L earlier and add 65 ~ 75g amount of sodium chloride than in secondary filtrating, adding sodium-chlor; And then regulate pH to 1.9 ~ 2.1, then leave standstill 15 ~ 25min under the room temperature;
6), with the step 5) gains under 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, collect filtrating;
7), add 220 ~ 240g amount of sodium chloride according to every 1L filtrating (for the filtrating of step 6) gained) earlier and add sodium-chlor than in filtrating; And then regulate pH to 1.9 ~ 2.1, then leave standstill 15 ~ 25min under the room temperature;
8), the gains of step 7) are centrifugal under room temperature, with the resolution of precipitate of gained in PBS damping fluid (pH7.4) or zero(ppm) water;
Remarks explanation: the minimum requirement ability of the consumption of PBS damping fluid (pH7.4) or zero(ppm) water dissolution precipitation; Generally speaking, PBS damping fluid (pH7.4) or the zero(ppm) water of the fresh milk of 1000ml about as raw material adapted 100 ml.
9), under the room temperature, the solution of step 8) gained was carried out ultrafiltration 2 ~ 8 hours with the filter membrane of molecular weight cut-off 10000; The trapped fluid of gained gets freeze-drying beta-lact oglobulin powder through freeze-drying.
As the improvement that from raw dairy, separates the method for beta-lact oglobulin of the present invention:
Freeze-drying beta-lact oglobulin powder is purified: use C8 reversed-phase bonded silica chromatographic column, carry out gradient elution as moving phase with second eyeball-water; The 214nm wavelength detects, and gets A type beta-lact oglobulin and Type B beta-lact oglobulin respectively.
As further improvements in methods of from raw dairy, separating beta-lact oglobulin of the present invention:
Step 1) is: with fresh milk with 3500 ~ 4500g, 3 ~ 5 ℃, centrifugal 25 ~ 35min, 4 pull-up fat filtered through gauze;
Step 3) is: filtrate in 3 ~ 5 ℃ centrifugal 15 ~ 25 min under 4500 ~ 5500g, 4 pull-up fat filtered through gauze after will handling first;
Step 6) is: with the step 5) gains in 3 ~ 5 ℃, centrifugal 15 ~ 25min under 8000 ~ 12000g, 4 pull-up fat filtered through gauze;
Step 8) is: with the centrifugal 15 ~ 25min of gains 9000 ~ 11000g under room temperature of step 7).
As further improvements in methods of from raw dairy, separating beta-lact oglobulin of the present invention:
Step 2), all use the salt acid for adjusting pH value of 0.8 ~ 1.2 M in the step 4);
Step 5) and step 7) are all used the salt acid for adjusting pH value of 1.8 ~ 2.2M.
As further improvements in methods of from raw dairy, separating beta-lact oglobulin of the present invention:
Freeze-drying in the step 9) is: under-40 ℃ ~-50 ℃ with the trapped fluid freeze-drying to constant weight.
Method of from raw dairy, separating beta-lact oglobulin of the present invention, be with cow's milk behind centrifugal degreasing, through conciliation pH, saltouing obtains beta-lact oglobulin solution, with freeze-drying after the desalination and concentration by ultrafiltration, obtains the beta-lact oglobulin lyophilized powder; The employing HPLC detects, and beta-lact oglobulin lyophilized powder purity is greater than 95%.
The freeze-drying beta-lact oglobulin powder of gained of the present invention is identified albumen from the molecular weight angle: adopt 12-20% concentration sodium laurylsulfonate (SDS)-polyacrylamide gel electrophoresis (PAGE); Coomassie brilliant blue staining; With standard control, confirm that the sub-molecular weight of target protein is 18.2kD.
The provided by the invention use to saltout and the beta-lact oglobulin separation purification method of ultrafiltration as core provides a kind of quick, low-cost, highly purified beta-lact oglobulin separation purification method.
In sum, adopt method of the present invention from fresh milk, to isolate beta-lact oglobulin,, can obtain highly purified beta-lact oglobulin in conjunction with the ultrafiltration desalination through Acid precipitation and the method for saltouing.Present method has improved the beta-lact oglobulin separation efficiency, for other aspect researchs of beta-lact oglobulin and use the fine starting material are provided.
Description of drawings
Do further explain below in conjunction with the accompanying drawing specific embodiments of the invention.
Fig. 1 is the HPLC color atlas of different genotype β-LG after purifying.
Embodiment
Embodiment 1, a kind of method of from raw dairy, separating beta-lact oglobulin, with the fresh milk of 1000ml as raw material; Carry out following steps successively:
1), with fresh milk with 4000g, 4 ℃, centrifugal 30min, 4 pull-up fat filtered through gauze, thus remove dairy fats, collect the filtrating first of gained;
2), filtrating is transferred pH to 4.6 with 1 M hydrochloric acid first, leaves standstill 30min under the room temperature; Filtrate first after must handling;
3), filtrate 4 ℃ first after will handling, centrifugal 20 min under the 5000g, 4 pull-up fat filtered through gauze, the filtrating of gained is repeated above-mentioned centrifugal and absorbent gauze filtration treatment (that is, in 4 ℃, centrifugal 20 min under the 5000g, 4 pull-up fat filtered through gauze), secondary filtrating;
4), regulate the pH to 2.0 of secondary filtrating with 1M hydrochloric acid, secondary filtrating after must handling; The volume of secondary filtrating after the recording processing;
5) secondary filtrating is added 70g amount of sodium chloride ratio after handling according to every 1L, earlier, in secondary filtrating, adds sodium-chlor; And then regulate pH to 2.0 with the hydrochloric acid of 2 M, then leave standstill 20min under the room temperature;
6), with the step 5) gains in 4 ℃, centrifugal 20min under the 10000g, 4 pull-up fat filtered through gauze are collected filtrating;
7), add sodium-chlor than in filtrating according to adding the 230g amount of sodium chloride in every 1L filtrating (step 6) gained) earlier; Transfer pH 2.0 with the hydrochloric acid of 2 M then, leave standstill 20min under the room temperature;
8), under the gains room temperature with step 7), the centrifugal 20min of 10000g gets deposition, is dissolved in the 100 ml PBS damping fluids (pH7.4);
9), under the room temperature, with solution ultrafiltration (membrane retention molecular weight 10000) 2 h of step 8) gained, the trapped fluid of gained in-45 ℃ of freeze-drying to constant weight; Get freeze-drying beta-lact oglobulin powder (beta-lactoglobulin content accounts for more than 95% of total protein).
The fresh milk of every 1000ml finally can get the freeze-drying beta-lact oglobulin powder of 2.7g and (also claim: the beta-lact oglobulin lyophilized powder).
One, above-mentioned freeze-drying beta-lact oglobulin powder is identified albumen from the molecular weight angle:
Adopt 12-20% concentration sodium laurylsulfonate (SDS)-polyacrylamide gel electrophoresis (PAGE), coomassie brilliant blue staining with standard control, confirms that the sub-molecular weight of albumen of above-mentioned freeze-drying beta-lact oglobulin powder is 18.2kD.
Two, with the purity of C8 reversed-phase bonded silica chromatogram column analysis beta-lact oglobulin:
Gained beta-lact oglobulin lyophilized powder purity adopts HPLC to detect, and concrete grammar is:
Mobile phase A: volumetric concentration 0.1% trifluoroacetic acid aqueous solution;
Mobile phase B: volumetric concentration 0.1% trifluoroacetic acid acetonitrile solution;
Protein lysate: 0.1M BisTris (2, the two dihydroxymethyl aniline of 2-), 6M Guanidinium hydrochloride, 5.37mM Trisodium Citrate, the mixing solutions of 19.5mM WR 34678 (using the zero(ppm) water constant volume);
Diluted protein solution: with the mobile phase A is the 4.5M guanidine hydrochloride solution of solvent;
Chromatographic column: C8 post (that is C8 reversed-phase bonded silica chromatographic column);
Detect wavelength: 214nm;
Detected temperatures: 45 ℃;
Sample size: 10 μ L;
In ultrapure water, being configured to concentration is that 10mg/mL solution is frozen in-20 ℃ with freeze-drying beta-lact oglobulin powder dissolution; As freezing sample;
In freezing sample, add isopyknic protein lysate, sample melts back vibration 10s mixing, and room temperature leaves standstill 1h; With the mixing solutions 16000g that leaves standstill gained, 4 ℃ of centrifugal 5min; Thereby remove impurity;
Get bottom solution adding diluted protein solution and dilute, get diluent, the volume ratio 1:3 of bottom solution and diluted protein solution;
Get 10 μ L diluents, the gradient elution that is described in table 1 below:
The gradient elution program that table 1, milk-protein are analyzed
The flow velocity of the washing lotion of above-mentioned gradient elution is: 0.5 ml/min.
The elutriant of collecting 32 ~ 34min time period is elutriant A (corresponding is the Type B beta-lact oglobulin); Collect the elutriants of 34 ~ 36 time periods is elutriant B (corresponding is A type beta-lact oglobulin); Above-mentioned elutriant A and elutriant B are handled respectively as follows: elutriant is carried out ultrafiltration (molecular weight 10000 dalton) 2h or dialysis (molecular weight 10000 dalton) is spent the night except that freshen, with the trapped fluid of gained in-45 ℃ of freeze-drying to constant weight; Get freeze-drying A type beta-lact oglobulin powder 55ug and Type B beta-lact oglobulin powder 35ug (purity is more than 98%).
The HPLC color atlas of above-mentioned A type beta-lact oglobulin, Type B beta-lact oglobulin and biased sample (that is, the back different genotype β-LG that purifies also is the freeze-drying beta-lact oglobulin powder of embodiment 1 gained) is as shown in Figure 1.
The A type, the β-LG of Type B and mixed type calculates its purity greater than 95% according to the peak area ratio.
Therefore, the A type beta-lact oglobulin powder of the fresh milk of the every 1000ml 1.53g that finally can get, the Type B beta-lact oglobulin powder of 1.01g.
Comparative Examples 1, make amount of sodium chloride in the step 5) into 50g, all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 80.7%) of 2.1 g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 0.93g, the Type B beta-lact oglobulin powder of 0.58 g.
Comparative Examples 2, make amount of sodium chloride in the step 5) into 90g, all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 67.8%) of 2.5 g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 0.89g, the Type B beta-lact oglobulin powder of 0.48g.
Comparative Examples 3, make amount of sodium chloride in the step 7) into 300g, all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 88.7%) of 2.5 g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 1.12g, the Type B beta-lact oglobulin powder of 0.78g.
Comparative Examples 4, make amount of sodium chloride in the step 7) into 180g, all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 72.8%) of 2.7g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 0.98g, the Type B beta-lact oglobulin powder of 0.59g.
Comparative Examples 5, cancellation step 2), all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 58.2%) of 2.3g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 0.73g, the Type B beta-lact oglobulin powder of 0.46g.
Comparative Examples 6, cancellation step 5), all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 67.4%) of 1.8g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 0.61g, the Type B beta-lact oglobulin powder of 0.39g.
Comparative Examples 7, cancellation step 7), all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder of 0g.
Comparative Examples 8, cancellation step 9) in ultrafiltration, all the other are equal to embodiment 1.
The fresh milk of every 1000ml finally can get the beta-lact oglobulin powder (purity is 85.2%) of 2.7g.
The fresh milk of every 1000ml finally can get the A type beta-lact oglobulin powder of 1.26g, the Type B beta-lact oglobulin powder of 0.81g.
At last, it is also to be noted that what more than enumerate only is several specific embodiments of the present invention.Obviously, the invention is not restricted to above embodiment, many distortion can also be arranged.All distortion that those of ordinary skill in the art can directly derive or associate from content disclosed by the invention all should be thought protection scope of the present invention.
Claims (5)
1. from raw dairy, separate the method for beta-lact oglobulin, it is characterized in that comprising the steps:
1), with fresh milk in 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, thereby remove dairy fats, filtrating first;
2), filtrating is regulated pH to 4.5 ~ 4.7 first, leaves standstill 20 ~ 40min under the room temperature; Filtrate first after must handling;
3), filtrate first after will handling in 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, the filtrating of gained is repeated centrifugal and the absorbent gauze filtration treatment above-mentioned 3 ~ 5 ℃ under, must filtrate by secondary;
4), secondary filtrating is regulated pH to 1.9 ~ 2.1, secondary filtrating after must handling;
5), handle back secondary filtrating according to every 1L earlier and add 65 ~ 75g amount of sodium chloride than in secondary filtrating, adding sodium-chlor; And then regulate pH to 1.9 ~ 2.1, then leave standstill 15 ~ 25min under the room temperature;
6), with the step 5) gains under 3 ~ 5 ℃ through centrifugal and absorbent gauze filtration treatment, collect filtrating;
7), add 220 ~ 240g amount of sodium chloride according to every 1L filtrating earlier and add sodium-chlor than in filtrating; And then regulate pH to 1.9 ~ 2.1, then leave standstill 15 ~ 25min under the room temperature;
8), the gains of step 7) are centrifugal under room temperature, with the resolution of precipitate of gained in PBS damping fluid or zero(ppm) water;
9), under the room temperature, the solution of step 8) gained was carried out ultrafiltration 2 ~ 8 hours with the filter membrane of molecular weight cut-off 10000; The trapped fluid of gained gets freeze-drying beta-lact oglobulin powder through freeze-drying.
2. method of from raw dairy, separating beta-lact oglobulin according to claim 1 is characterized in that:
Freeze-drying beta-lact oglobulin powder is purified: use C8 reversed-phase bonded silica chromatographic column, carry out gradient elution as moving phase with second eyeball-water; Get A type beta-lact oglobulin and Type B beta-lact oglobulin respectively.
3. method of from raw dairy, separating beta-lact oglobulin according to claim 1 and 2 is characterized in that:
Said step 1) is: with fresh milk with 3500 ~ 4500g, 3 ~ 5 ℃, centrifugal 25 ~ 35min, 4 pull-up fat filtered through gauze;
Said step 3) is: filtrate in 3 ~ 5 ℃ centrifugal 15 ~ 25 min under 4500 ~ 5500g, 4 pull-up fat filtered through gauze after will handling first;
Said step 6) is: with the step 5) gains in 3 ~ 5 ℃, centrifugal 15 ~ 25min under 8000 ~ 12000g, 4 pull-up fat filtered through gauze;
Said step 8) is: with the centrifugal 15 ~ 25min of gains 9000 ~ 11000g under room temperature of step 7).
4. method of from raw dairy, separating beta-lact oglobulin according to claim 3 is characterized in that:
Said step 2), all use the salt acid for adjusting pH value of 0.8 ~ 1.2 M in the step 4);
Step 5) and step 7) are all used the salt acid for adjusting pH value of 1.8 ~ 2.2M.
5. method of from raw dairy, separating beta-lact oglobulin according to claim 4 is characterized in that:
Freeze-drying in the said step 9) is: under-40 ℃ ~-50 ℃ with the trapped fluid freeze-drying to constant weight.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN2012102317977A CN102746395A (en) | 2012-07-04 | 2012-07-04 | Method for separating beta-lactoglobulin from raw milk |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN2012102317977A CN102746395A (en) | 2012-07-04 | 2012-07-04 | Method for separating beta-lactoglobulin from raw milk |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN102746395A true CN102746395A (en) | 2012-10-24 |
Family
ID=47026930
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN2012102317977A Pending CN102746395A (en) | 2012-07-04 | 2012-07-04 | Method for separating beta-lactoglobulin from raw milk |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN102746395A (en) |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105348379A (en) * | 2015-12-16 | 2016-02-24 | 新希望双喜乳业（苏州）有限公司 | Method for extracting beta-lactoglobulin from milk |
| CN105732794A (en) * | 2015-11-06 | 2016-07-06 | 广西大学 | Method of recyclable large-scale separation of [beta]-lactoglobulin |
| CN106798009A (en) * | 2015-11-26 | 2017-06-06 | 内蒙古伊利实业集团股份有限公司 | A kind of acidified milk for adding gelation beta lactoglobulin product and preparation method thereof |
| CN107298711A (en) * | 2017-06-08 | 2017-10-27 | 江苏华冠生物技术股份有限公司 | Allergenic factor beta lactoglobulin in a kind of column chromatography method separation colostrum |
| CN111440234A (en) * | 2020-04-24 | 2020-07-24 | 浙江大学 | Preparation method of buffalo milk β -casein antioxidant |
| CN112770637A (en) * | 2018-06-27 | 2021-05-07 | 阿尔拉食品公司 | Novel method for preparing compositions enriched in alpha-lactalbumin, related products and use in e.g. infant formulas |
| CN113925124A (en) * | 2021-09-29 | 2022-01-14 | 五邑大学 | Dried orange peel essential oil emulsion and preparation method and application thereof |
| CN116982656A (en) * | 2023-08-01 | 2023-11-03 | 安徽天凯生物科技有限公司 | Method and device for separating components in milk and dairy products |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1606917A (en) * | 2003-10-13 | 2005-04-20 | 彭平 | Method for extracting lactalbumin and separating different active ingredient of lactalbumin |
| CN1817149A (en) * | 2005-12-01 | 2006-08-16 | 徐跃 | Complete separating process for fresh liquid milk |
| CN102286096A (en) * | 2011-07-08 | 2011-12-21 | 上海交通大学 | Scale purification method for lactalbumin |
-
2012
- 2012-07-04 CN CN2012102317977A patent/CN102746395A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1606917A (en) * | 2003-10-13 | 2005-04-20 | 彭平 | Method for extracting lactalbumin and separating different active ingredient of lactalbumin |
| CN1817149A (en) * | 2005-12-01 | 2006-08-16 | 徐跃 | Complete separating process for fresh liquid milk |
| CN102286096A (en) * | 2011-07-08 | 2011-12-21 | 上海交通大学 | Scale purification method for lactalbumin |
Non-Patent Citations (2)
| Title |
|---|
| 《中国乳品工业》 20100125 段翠翠等 从WPC中分离beta-lactoglobulin的方法 第38卷, 第1期 * |
| 段翠翠等: "从WPC中分离β-lactoglobulin的方法", 《中国乳品工业》 * |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105732794A (en) * | 2015-11-06 | 2016-07-06 | 广西大学 | Method of recyclable large-scale separation of [beta]-lactoglobulin |
| CN105732794B (en) * | 2015-11-06 | 2020-07-07 | 广西大学 | Method for circularly separating β -lactoglobulin in large scale |
| CN106798009A (en) * | 2015-11-26 | 2017-06-06 | 内蒙古伊利实业集团股份有限公司 | A kind of acidified milk for adding gelation beta lactoglobulin product and preparation method thereof |
| CN106798009B (en) * | 2015-11-26 | 2020-10-20 | 内蒙古伊利实业集团股份有限公司 | Fermented milk added with gel beta-lactoglobulin product and preparation method thereof |
| CN105348379A (en) * | 2015-12-16 | 2016-02-24 | 新希望双喜乳业（苏州）有限公司 | Method for extracting beta-lactoglobulin from milk |
| CN107298711A (en) * | 2017-06-08 | 2017-10-27 | 江苏华冠生物技术股份有限公司 | Allergenic factor beta lactoglobulin in a kind of column chromatography method separation colostrum |
| CN112770637A (en) * | 2018-06-27 | 2021-05-07 | 阿尔拉食品公司 | Novel method for preparing compositions enriched in alpha-lactalbumin, related products and use in e.g. infant formulas |
| CN111440234A (en) * | 2020-04-24 | 2020-07-24 | 浙江大学 | Preparation method of buffalo milk β -casein antioxidant |
| CN111440234B (en) * | 2020-04-24 | 2021-07-13 | 浙江大学 | Preparation method of buffalo milk beta-casein antioxidant |
| CN113925124A (en) * | 2021-09-29 | 2022-01-14 | 五邑大学 | Dried orange peel essential oil emulsion and preparation method and application thereof |
| CN116982656A (en) * | 2023-08-01 | 2023-11-03 | 安徽天凯生物科技有限公司 | Method and device for separating components in milk and dairy products |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN102746395A (en) | Method for separating beta-lactoglobulin from raw milk | |
| US9181316B2 (en) | Method for isolating osteopontin using feeds containing CMP or casein species | |
| WO2005110112A9 (en) | Methods and compositions involving whey protein isolates | |
| US20220295809A1 (en) | Methods and compositions for protein concentration | |
| US6555659B1 (en) | Process for isolating glycomacropeptide from dairy products with a phenylalanine impurity of 0.5% w/w | |
| JP5709353B2 (en) | Novel milk protein fraction and its use for the prevention or treatment of chronic inflammatory diseases | |
| DK2595494T3 (en) | Methods for fractionating whey protein isolates | |
| CN1663961A (en) | Technology for separating and purifying lactoferritin from cow colostrum | |
| RU2416243C2 (en) | Method of extracting low molecular peptides | |
| CN104513305B (en) | A kind of purification process of lactalbumin | |
| WO2002074790A1 (en) | Large scale production of low fat and sds gel pure kappa-casein glycomacropeptides (gmp) from bovine deproteinized whey | |
| NZ614874B2 (en) | Method for isolating osteopontin using concentrated feeds | |
| NZ614872B2 (en) | Method for isolating osteopontin using feeds containing cmp or casein species |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C12 | Rejection of a patent application after its publication | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20121024 |