Molecular cloning，expression and identification of recombinant hyaluronan synthase from Pasteurella multocida

Aim ：To set a suitable route for efficient expression and purification of recombinant hyaluronan synthase from Pasteurella multocida(rPmHAS). Methods ：Coding sequences were cloned and expressed in Escherichia coli strain of BL-21(DE3).Then rPmHAS was purified through a simple Ni-affinity chromatography and identified by hyaluronic acid binding protein (HABP) based ELISA assay. Results ：High yield expression of functional rPmHAS exceeding the highest production reported hitherto was achieved，and the purity of rPmHAS was as high as 90%. Conclusion ：In this study，an optimized system of the expression，purification and identification route for large scale preparation of rPmHAS was established，which will be helpful for accelerating further study of PmHAS and facilitating fine researches on peculiar hyaluronic acid with special properties.