Studies on the β-Galactosidase from Gram──Gatalytic Reaction Kinetics of ONPG Hydrolysis and the Chemical Modification of Activity Sites

Abstract

Abstract: The catalytic properties of β-galactosidaseⅠand Ⅱpurified from gram germination seeds as ONPGhydrolysis catalysts were investigated.According to the Michaelis Menten mechanism of enzyme catalytic reaction,the kinetic parameters K_M,r_m and E_a of catalytic hydrolysis reaction of ONPG were measured.By using of various chemical dressing reagents for enzyme,we studied the function groups of β-galactosidaseⅠ.The relationship between the function groups and catalytic activity of enzyme revealed that hydrosulphonyl and tryptophan existed in β-galactosidase Ⅰand they were the composition groups in the active site of β-galactosidaseⅠfor the catalytic hydrolysis reaction of ONPG.

Key words: Galactosidase, Gram, Chemical modification, Catalytic hydrolysis, Reaction kinetics

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LI Xu-Yuan, ZHAO Ke-Hao, MEN Yan-Fa, MA Jian-Tai. Studies on the β-Galactosidase from Gram──Gatalytic Reaction Kinetics of ONPG Hydrolysis and the Chemical Modification of Activity Sites[J]. Chem. J. Chinese Universities, 1996, 17(10): 1555.

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Studies on the β-Galactosidase from Gram──Gatalytic Reaction Kinetics of ONPG Hydrolysis and the Chemical Modification of Activity Sites

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