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Preparation method of low-molecular weight collagen

A technology of collagen and low molecular weight, applied in peptide preparation methods, chemical instruments and methods, organic chemistry, etc.

Inactive Publication Date: 2015-01-14
广东中大南海海洋生物技术工程中心有限公司
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

weighing

Method used

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Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] Extraction of Collagen from Cod Skin

[0024] (1) Removal of fish skin miscellaneous protein, that is, non-collagen protein: Weigh 30g of cod skin and add 0.1M NaOH at 1:30 (g / ml) to soak for 24 hours at 4 degrees Celsius, and repeatedly soak with double distilled water until neutral , drained. Weighs 24g.

[0025] (2) Removal of fish skin fat: Remove miscellaneous protein cod skin by adding 10% n-butanol at 1:30 (g / ml) and soaking at 4 degrees Celsius for 24 hours, repeatedly rinsing with double distilled water until neutral, and filtering to dry. Weighing is 18g.

[0026] (3) Extraction of cod skin collagen: add double distilled water by 10 times of volume through the fish skin powder of above-mentioned treatment, add papain (pH is about 7 the best) by the ratio of 10%, 37 degrees Celsius (being the content of papain) Optimum active temperature) water bath for 12h, stirring once every 30min. Pour into the pre-weighed filter paper, completely filter dry, weigh, and...

Embodiment 2

[0029] According to Example 1, the molecular sieve chromatography separation and purification of the sample collagen enzymatic hydrolysis polypeptide liquid was obtained

[0030] Separation and purification of collagen polypeptides: Sephadex G-25 is used to separate and purify complex polypeptides, and the separated components are measured at a wavelength of 221nm.

[0031] (1) Selection of gel

[0032] Select G-25 dextran gel according to the molecular weight of the chromatographic material

[0033] (2) Pretreatment of the gel

[0034] Weigh an appropriate amount of gel and add excess buffer to fully expand in the refrigerator (or room temperature), or cook in boiling water. The expansion time should be determined according to different types of gel. In this experiment, 50 g of gel was weighed and swelled for 24 hours. In order to make the particles uniform, flotation is required, that is, after adding gel particles, stir gently, let stand for 20 minutes, pour out the prec...

Embodiment 3

[0040] Ion-exchange chromatography separation and purification experiment of sample obtained according to Example 2

[0041] The operation process is as follows:

[0042] Packing DEAE pretreatment→wet column packing→equilibrium column→column head sample loading→gradient elution→collect elution peak→detect peak protein concentration

[0043] (1) Pretreatment of filler DEAE

[0044] Weigh a certain amount of DEAE cellulose powder, soak it in distilled water for 2-4 hours, and carry out flotation, pour off the upper layer of water, add distilled water to wash it, dry it with a vacuum pump, soak and wash it with 0.5mol / L HCl solution for 0.5 hours , drained, and washed with a large amount of distilled water until nearly neutral. Then soak and wash with 0.5mol / L NaOH solution for 0.5h, drain, and wash with a large amount of distilled water until it is nearly neutral. However, it was soaked in 0.5mol / L HCl solution, modified, drained, and washed with distilled water until it was ...

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Abstract

The invention discloses a preparation method of low-molecular weight collagen. The preparation method of the low-molecular weight collagen comprises pre-treatment, molecular sieve chromatography and ion exchange column separation. Collagen is an important functional factor in a health product, sources, technology and molecular weight become main factors for influencing collagen effects, and molecular weight distribution is directly related to technology. Relative molecular weight is an important index of hydrolyzed collagen and needs to be researched deeply so that a relationship between the relative molecular weight of hydrolyzed collagen and activity of hydrolyzed collagen is ensured. Leftover of fish skin such as cod skin and tilapia skin is orderly subjected to fish-skin impurity protein removal, fish-skin fat removal and fish-skin collagen enzymolysis, and the obtained sample collagen zymolytic polypeptide liquid is subjected to molecular sieve chromatographic separation purification and ion exchange chromatographic separation purification so that high-purity collagen samples having different molecular weights are obtained.

Description

technical field [0001] The invention relates to a preparation method for obtaining low molecular weight collagen through pretreatment, molecular sieve chromatography and ion exchange column separation. Background technique [0002] Collagen is an important functional factor in health care products. It is planned to conduct exploratory experiments on the main factors affecting the quality of collagen. The main factors affecting the efficacy of collagen are source, process and molecular weight, and the distribution of molecular weight is directly related to the process. The relative molecular weight is an important indicator of the quality of hydrolyzed collagen, and it needs to be studied in depth to determine the relationship between the relative molecular weight and activity of hydrolyzed collagen. In addition, the existing functional literature shows that products with different amino acid compositions and molecular weights have different cosmetic effects, and these need ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12P21/06C07K1/18C07K1/16
Inventor 不公告发明人
Owner 广东中大南海海洋生物技术工程中心有限公司
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