Modification of Cellulase-Chitosanase Bifunctional Enzyme by Diethylpyrocarbonate and 1-Ethyl-3-carbodiimide

Abstract

Abstract: The cellulase-chitosanase bifunctional enzyme(CCBE) was modified with diethylpyrocarbonate(DEPC) and 1-ethyl-3-carbodiimide(EDC) respectively. The kinetic analysis of the CCBE modification by DEPC revealed that about one mole histidine(His) residue is essential for both cellulase activity and chitosanase activity of one mole CCBE. Treatment of inactivated enzyme with hydroxylamine results in nearly complete restoration of original activity,which confirms the abovementioned conclusion. The result of the modification of CCBE by EDC showed that the number of reactive carboxylate for both its cellulase activity and chitosanase activity center is one.

Key words: bifuctional enzyme, histidine residue, carboxylate, chemical modification

LIU Jing, XIA Wen-Shui. Modification of Cellulase-Chitosanase Bifunctional Enzyme by Diethylpyrocarbonate and 1-Ethyl-3-carbodiimide[J]. FOOD SCIENCE, 2008, 29(8): 460-463.

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Modification of Cellulase-Chitosanase Bifunctional Enzyme by Diethylpyrocarbonate and 1-Ethyl-3-carbodiimide

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