Isolation, Purification And Structural Characterization Of Recombinant Human Collagen
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Abstract
Abstract Pichia pastoris genetically engineered strain GS115/pPIC9KG6 was used for high-density fermentation to obtain extracellular secreted recombinant human-source collagen (RHSC). SDS-PAGE electrophoresis analysis proved that RHSC has a definite molecular mass , respectively about 56 kDa protein monomer and 112 kDa dimer. In the experiment, the fermentation supernatant of the engineering bacteria was purified by a combination of dialysis method, salt precipitation and column chromatography. The results are as follows: (1) Dialysis Method – the optimal conditions are 4¡ãC and dialysis for 24 hours. The recovery rate of the RHSC monomer and dimer mixture is close to 100% and the purity is 82.5%. (2) Salting out-column chromatography combined method – the fermentation supernatant is passed through After 40% saturation ammonium sulfate precipitation and purification with Sephadex G100, the dimer was obtained and reached electrophoretic purity. The structure of the separated and purified RHSC was characterized by DSC, ultraviolet spectrum, infrared spectrum and nuclear magnetic resonance spectrum, and compared with standard type III collagen. Comparison determined that RHSC has the characteristic structure of type III collagen.
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