Technology of preparing acid-soluble bovine tendo calcaneus collagen by freeze thawing-ultrasonic method

Abstract

The invention relates to a technology of preparing acid-soluble bovine tendo calcaneus collagen by a freeze thawing-ultrasonic method. The technology comprises the specific steps of: (1) bovine tendo calcaneus pretreatment: removing impurities from fresh bovine tendo calcaneus, soaking with normal saline, washing with pure water, freezing, slicing and airing, (2) swelling: putting and soaking aired bovine tendo calcaneus slices in an acetic acid solution for swelling, (3) beating: adding pure water into a swelled bovine tendo calcaneus suspension, performing mechanical beating to obtain crude slurry, (4) freeze thawing-ultrasonic: freezing the beaten bovine tendo calcaneus crude slurry, then performing ultrasonic treatment, repeating the freeze thawing-ultrasonic process to obtain a crude collagen extract, and (5) purification: performing filtering, centrifuging, salt precipitation, dialysis and freeze drying on the crude collagen extract to obtain the collagen product. The extraction method of the bovine tendo calcaneus collagen is simple and convenient and low in cost, the extraction rate of the collagen is increased without using enzyme, the purity of the obtained collagen is high, and a natural structure of the collagen is reserved. The prepared collagen can be applied to industries of medicine, cosmetics and the like.

Description

technical field

[0001] The invention relates to a process for preparing acid-soluble bovine Achilles tendon collagen by a freeze-thaw-ultrasonic method, in particular to a process for extracting natural collagen by a non-enzymatic method. The invention belongs to the technical field of collagen extraction in organisms. Background technique

[0002] The skin, bones, and tendons of vertebrates contain a large amount of collagen. There are various types, but type I collagen is the most abundant and widely used. The source of bovine Achilles tendon is rich, and the content of type I collagen is very high, which is a good source of raw material for extracting type I collagen. Type I collagen molecules are composed of three peptide chains coiled to form a unique triple helical structure, each chain contains a large number of repeated Gly-X-Y amino acid sequences, and the content of proline and hydroxyproline is relatively high. Collagen molecules contain a large number of hydro...