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Preparation and characterization of recombinant human-source collagen / 生物工程学报
Chinese Journal of Biotechnology ; (12): 319-326, 2019.
Article in Chinese | WPRIM | ID: wpr-771374
ABSTRACT
This study aimed to obtain a recombinant human-source collagen for industrialization. First, based on the Gly-X-Y sequence of human type I collagen, we optimized the hydrophilic Gly-X-Y collagen peptide, designed the human collagen amino acid sequence and the corresponding nucleotide sequence. Next, the expression vector pPIC9K-COL was constructed via endonuclease digestion technology. We obtained an engineering strain of human-source collagen by electrotransforming Pichia pastoris, and then it was fermented, purified and identified. As a result, the expression level reached 4.5 g/L and the purity was over 95%. After amino acid N-terminal sequencing, molecular weight analysis, amino acid analysis and collagenase degradation test, we confirmed that the obtained collagen was consistent with designed primary structure of human-source collagen. After freeze-drying, we analyzed the collagen by scanning electron microscope and cell cytotoxicity, confirming that the collagen has porous fiber reticular structure and superior cytocompatibility. This indicates that human-source collagen has potential to be applied as biomedical material. In conclusion, we successfully obtained the expected human-source collagen and laid a foundation to its further application.
Subject(s)

Full text: Available Index: WPRIM (Western Pacific) Main subject: Pichia / Biocompatible Materials / Recombinant Proteins / Collagen / Amino Acid Sequence / Freeze Drying Limits: Humans Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2019 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Pichia / Biocompatible Materials / Recombinant Proteins / Collagen / Amino Acid Sequence / Freeze Drying Limits: Humans Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2019 Type: Article