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dc.contributor.authorXie, XL
dc.contributor.author谢晓兰
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.date.accessioned2011-10-09T10:12:10Z
dc.date.available2011-10-09T10:12:10Z
dc.date.issued2004
dc.identifier.citationBIOCHEMISTRY-MOSCOW,volume69,issue12,pp1365-1371zh_CN
dc.identifier.issn0006-2979
dc.identifier.urihttp://dx.doi.org/doi:10.1007/s10541-005-0082-7
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10881
dc.description.abstractbeta-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-beta-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 substrate 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.zh_CN
dc.language.isoenzh_CN
dc.publisherMAIK NAUKA/INTERPERIODICAzh_CN
dc.subjectbeta-N-acetyl-D-glucosaminidasezh_CN
dc.subjectPenaeus vannameizh_CN
dc.subjectdioxanezh_CN
dc.subjectinactivation kineticszh_CN
dc.titleInactivation kinetics of beta-n-acetyl-d-glucosaminidase from prawn (Penaeus vannamei) in dioxane solutionzh_CN
dc.typeArticlezh_CN


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