Chinese Journal of Catalysis ›› 2009, Vol. 30 ›› Issue (7): 673-678.

• Articles • Previous Articles     Next Articles

Characterization of Key Amino Acid Residues in Active Sites of Inulinase from Bacillus smithii T7 by Chemical Modification

LIU Bin, WANG Jingyun*, BAO Yongming, ZHANG Fan, AN Lijia   

  1. Department of Bioscience and Biotechnology, School of Environmental and Biological Science and Technology, Dalian University of Tech-nology, Dalian 116024, Liaoning, China
  • Received:2009-07-25 Online:2009-07-25 Published:2013-04-24

Abstract: Chemical modification demonstrated that one histidine and one carboxylate residues in the active site of endo-inulinase from Bacillus smithii T7 play a key role in the catalytic function. Two tryptophan residues are necessary for the enzyme activity and are also important for the enzyme’s thermal stability.

Key words: inulinase, chemical modification, active site, amino acid residue, catalysis