Preparation And Regional Stability Of Recombinant Collagen

Collagen is one of the most important structural proteins in the human body.It has a characteristic(Gly-X-Y)n repeating sequence,and wherein the amino acids at the X and Y positions are proline and hydroxyproline.Non-animal-derived recombinant collagen has the advantages of low immunogenicity and the like,and is therefore one of the ideal materials for biomedical materials,compared with collagen extracted from animals.In this paper,three aspects of the preparation of recombinant collagen and regional stability were carried out:(1)large-scale culture of recombinant collagen.Optimization of culture conditions such as selection of culture medium,p H of culture environment and induction temperature.Making the yield of V-CL up to 14.3g / L.(2)the use of acid precipitation method to achieve one step purification V-CL.Compared with the traditional small-scale chromatography,acid deposition method is more simple,efficient,and no introduction of heavy metal ions,more environmentally friendly.(3)To study the proteolytic sequence of the hydrolyzate of the V-CL protein and compare it with the predicted stability characteristics.The proteolytic sequence determined by the experiment was consistent with the predicted stability characteristics,indicating that the proteolytic sequence of these proteolytic sites was determined by its structural stability.Since the digestion of collagen is usually associated with disease status,this study reveals the biodegradation pathways of collagen and related disease models.