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Cloning, Expression and Activity of an Endo-1,4-β-D-Glucanase from Pantoea ananatis

HOU Jinhui, ZHANG Xiang, QIAO Gaoxiang   

  1. College of Food Engineering, Xuzhou Institute of Technology, Xuzhou 221111, China
  • Online:2016-12-15 Published:2016-12-21

Abstract: The endo-1,4-β-D-glucanase gene from Pantoea ananatis was cloned and expressed in Escherichia coli. The
recombinant enzyme was purified with Ni-NTA affinity chromatography and its activity was analyzed. The results showed
that the recombinant glucanase gene contained a 1 002 bp-length open reading frame encoding two putative peptides of
334 amino acids. The expression of the recombinant enzyme in E. coli reached up to 50% of the total soluble protein. After
purification, the purity was higher than 95% and glucanase activity was as high as 2 245 U/mL.

Key words: endo-1,4-β-D-glucanase, prokaryotic expression, activity analysis

CLC Number: