Purifying type I collagen using two papain treatments and reducing and delipidation agents

Abstract

Purified collagen such a type I collagen is produced by a method containing steps of contacting collagen with a first proteolytic enzyme followed by contacting with a reducing agent and a second proteolytic enzyme. Preferably, the first and second proteolytic enzymes are papain and the reducing agent is sodium sulfide, dithiothreitol, glutathionine or sodium borohydride. In a further step, the purified collagen may be contacted with a delipidation agent such as a mixture of chloroform and methanol to produce delipidated collagen. The delipidated collagen may be filter-sterilized and contacted with a phosphorylation agent such as sodium trimetaphosphate to produce phosphorylated collagen. The delipidated collagen may also be treated by compressing, dehydrating, dispersing and drying to form collagen fibers. De-epithelializing of the collagen may carried out prior to treating with the first proteolytic enzyme. The collagen may be solubilized using a solubilizing agent such as acetic acid. The purified collagen is biocompatible and may be used in transplantation or hemostasis, and may be provided with compounds such as antimicrobials, antivirals, growth factors, anti-dehydration compounds and other compounds suitable for biomedical use.

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