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  • Chem Sci Trans., 2012, 1(2),  pp 347-354  

    DOI:10.7598/cst2012.4643

    Research Article

    Structure Analysis of a Highly Hydrophilic Recombinant Human-Source Gelatin

  • B. LIU, Y T. LEI and S L. YANG*
  • School of Environmental and Biological Engineering, Nanjing University of Science and Technology, Nanjing 210094, China
  • Abstract

    Collagen and gelatin is widely used as bio-polymer materials and medical materials. Currently, the direction is more and more clear that collagen-like peptide produced by chemical synthesis, and recombinant collagen and gelatin produced in various expression system constructed by gene engineering technique substitute for these products prepared by traditional methods. Based on the characteristic of collagenous domain of human type III collagen, a recombinant human-source gelatin monomeric gene was designed and synthesized. After a series of gene cutting/ligation and transformation, etc. then expressed it in Pichia pastoris. The expression pruduct was purified from fermentation supernatant by gel filtration chromatography, then amino acid analyses, MALDI-TOF-MS analyses, FTIR spectroscopy, circular dichroism spectroscopy and scanning electron microscope were used to analyze the protein structure. It was confirmed that recombinant human-source gelatin is similar to animal-derived gelatin in protein structure.

    Keywords

    Recombinant human-source gelatin, Pichia pastoris, chemical synthesis gene, structure analysis

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