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- W2378414755 abstract "β-N-Acetyl-D-glucosaminidase (NAGase, EC 3.2.1.52) catalyzes the cleavage of N-acetylglucosamine polymers. We previously purified this enzyme from pacific white shrimp (Penaeus vannamei). The effects of dimethyl sulfoxide(DMSO) on the enzyme activity for the hydrolysis of pNP-β-D-GlcNAc have been studied. The results show that DMSO, at appropriate concentrations, can lead to reversible inactivation of the enzyme, and the IC_ 50 is estimated to be 1.2 mol/L. The kinetics of inactivation of NAGase in DMSO solution has been studied using the kinetic method of the progress-substrate-reaction described by Tsou. The rate constants of inactivation have been determined. The results show that k_ +0 is much higher than k′_ +0 , indicating the free enzyme molecule is more fragile than the enzyme-substrate complex in the DMSO solution. These data suggested that the presence of the substrate offers marked protection of the enzyme against inactivation by DMSO." @default.
- W2378414755 created "2016-06-24" @default.
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- W2378414755 date "2005-01-01" @default.
- W2378414755 modified "2023-09-24" @default.
- W2378414755 title "Inactivation Kinetics of β-N-Acetyl-D-glucosaminidase from Pacific White Shrimp (Penaeus vannamei) by Dimethyl Sulfoxide" @default.
- W2378414755 hasPublicationYear "2005" @default.
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