Preparation And Characterization Of Recombinant Human Collagen
Keywords
Collagen, Human Origin, Pichia Pastoris, Biomaterials
Abstract
In order to obtain recombinant human collagen that can be industrially produced, the amino acid sequence and corresponding nucleotides of human collagen were designed based on the Gly-XY sequence of human type I collagen, preferably the hydrophilic Gly-XY collagen peptide segment. Sequence, use enzyme digestion technology to construct the pPIC9K-COL expression vector, electrotransform Pichia pastoris to obtain human collagen Pichia pastoris engineering strain, and conduct fermentation tank fermentation, purification and identification. The results showed that human collagen with an expression level of 4.5 g/L and a purity greater than 95% was obtained. After amino acid N-terminal sequencing, molecular weight determination, amino acid analysis and collagenase degradation test, it was determined that the obtained protein was consistent with the theoretical human origin. The primary structure of collagen is consistent; at the same time, after freeze-drying, scanning electron microscopy analysis and cytotoxicity tests were conducted on the collagen. It was determined that the freeze-dried human collagen product has a porous fiber network structure and excellent cytocompatibility, which indicates that it has the potential to be used as a biological The potential of medical materials
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Original research was done by Hou Zengmiao, Li Min, Li Xiaoying, Yang Xiaolin, Yang Jinfang, Zhao Jinli
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