Abstract
β-N-Acetyl-D-glucosaminidase (NAGase, EC 3.2.1.52) catalyzes the cleavage of N-acetylglucosamine polymers. It is in the composition of the chitinases and cooperates with endo-chitinase and exo-chitinase to disintegrate chitin into N-acetylglucosamine. In this work, the effects of dioxane on the enzyme activity for the hydrolysis of p-nitrophenyl-N-acetyl-β-D-glucosaminide from the prawn (Penaeus vannamei) have been studied. The results show that appropriate concentrations of dioxane can lead to reversible inactivation of the enzyme, and the IC50 is estimated to be 1.1 M. The kinetics of inactivation of NAGase in the appropriate concentrations of dioxane solution has been studied using the kinetic method of the sub-strate reaction. The rate constants of inactivation have been determined. The results show that the free enzyme molecule is more fragile than the enzyme—substrate complex in the dioxane solution. It is suggested that the presence of the substrate offers marked protection of this enzyme against inactivation by dioxane.
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Abbreviations
- NAGase:
-
β-N-acetyl-D-glucosaminidase
- pNP- β-D-GlcNAc:
-
p-nitrophenyl-N-acetyl-β-D-glucosaminide
- NaAc-HAc:
-
sodium acetate/acetate buffer
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Translated from Biokhimiya, Vol. 69, No. 12, 2004, pp. 1675–1682.
Original Russian Text Copyright © 2004 by XiaoLan Xie, QingXi Chen.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-093, June 27, 2004.
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Xie, XL., Chen, QX. Inactivation kinetics of β-N-acetyl-D-glucosaminidase from prawn (penaeus vannamei) in dioxane solution. Biochemistry (Moscow) 69, 1365–1371 (2004). https://doi.org/10.1007/s10541-005-0007-5
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DOI: https://doi.org/10.1007/s10541-005-0007-5