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dc.contributor.authorZhang, JP
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.contributor.authorWang, Q
dc.contributor.author王勤
dc.contributor.authorXie, JJ
dc.date.accessioned2011-09-16T08:59:20Z
dc.date.available2011-09-16T08:59:20Z
dc.date.issued2006
dc.identifier.citationBIOCHEMISTRY-MOSCOW,Volume 71, Pages s55-s59zh_CN
dc.identifier.issn0006-2979
dc.identifier.urihttp://dx.doi.org/doi:10.1134/S0006297906130098
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10752
dc.description.abstractbeta-N-Acetyl -D-glucosaminidase was purified from viscera of green crab (Scylla serrata) by extraction with 0.01 M Tris-HCl buffer (pH 7.5) containing 0.2 M NaCl, ammonium sulfate fractionation, and then chromatography on Sephadex G-100 and DEAE-cellulose (DE-32). The purified enzyme showed a single band on polyacrylamide gel electrophoresis, and the specific activity was determined to be 7990 U/mg. The molecular weight of the whole enzyme was determined to be 132.0 kD, and the enzyme is composed of two identical subunits with molecular mass of 65.8 kD. The optimum pH and optimum temperature of the enzyme for the hydrolysis of p-nitrophenyl-N-acetyl-beta-D-glucosaminide (pNP-NAG) were found to be at pH 5.6 and at 50 degrees C, respectively The study of its stability showed that the enzyme is stable in the pH range from 4.6 to 8.6 and at temperatures below 45 degrees C. The kinetic behavior of the enzyme in the hydrolysis of pNP-NAG followed Michaelis-Menten kinetics with K-m of 0.424 +/- 0.012 mM and V-max of 17.65 +/- 0.32 mu mol/min at pH 5.8 and 37 degrees C, and the activation energy was determined to be 61.32 kJ/mol. The effects of some metal ions on the enzyme were surveyed, and the results show that Na+ and K+ have no effects on the enzyme activity; Mg2+ and Ca2+ slightly activate the enzyme, while Ba2+, Zn2+, Mn2+, Hg2+, Pb2+, Cu2+, and Al3+ inhibit the enzyme to different extents.zh_CN
dc.language.isoenzh_CN
dc.publisherMAIK NAUKA/INTERPERIODICAzh_CN
dc.subjectenzymatic propertieszh_CN
dc.subjectbeta-N-acetyl-D-glucosaminidasezh_CN
dc.subjectpurificationzh_CN
dc.subjectScylla serratazh_CN
dc.titlePurification and some properties of beta-N-acetyl-D-glucosaminidase from viscera of green crab (Scylla serrata)zh_CN
dc.typeArticlezh_CN


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