FOOD SCIENCE ›› 2007, Vol. 28 ›› Issue (12): 340-344.

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Study on Active Site of L-arabinose Isomerase from Lactobacillus plantarum

 ZHANG  Hua, JIANG  Bo, PAN  Bei-Lei   

  1. 1.State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China; 2.Chinese Institute of Food Science and Technology, Beijing 100833, China; 3.Post-doctor Working station of Zhengzhou Sanquan Food Co. Ltd., Zhengzhou 450044, China
  • Online:2007-12-15 Published:2011-11-22

Abstract: The modification chemicals of NBS, PMSF, DEPC, EDC, TNBS, 2-mercaptoethanol and PCMB were used to reactwith L-arabinose isomerase from Lactobacillus plantarum. The L-arabinose isomerase could be inactivated with NBS, PMSF and DEPC. The tryptophan residues, serine residues and histidine residues might be involved in the active site of the enzyme. 4 mg/ml galactose could completely inhibit the inactivation of L-arabinose isomerase with NBS and PMSF, but the substrate showed no effect on the modification by DEPC. The results revealed that serine and tryptophan are positioned in the substrate binding site while histidine in the catalytic site.

Key words: Lactobacillus plantarum, L-arabinose isomerase, chemical modification, active site