Purification and Characterization of a Liver Chitinase from Golden Cuttlefish, Sepia esculenta

被引:3
作者
Nishino, Ryo [1 ]
Suyama, Akiyoshi [1 ]
Ikeda, Mana [1 ]
Kakizaki, Hiromi [1 ]
Matsumiya, Masahiro [1 ]
机构
[1] Nihon Univ, Dept Marine Sci & Resources, Coll Bioresource Sci, Fulisawa, Kanagawa 2520880, Japan
关键词
Chitinase; Purification; Characterization; Liver; Sepia esculenta;
D O I
10.1166/jcc.2014.1065
中图分类号
TB3 [工程材料学]; R318.08 [生物材料学];
学科分类号
0805 ; 080501 ; 080502 ;
摘要
A chitinase was purified from the liver of the golden cuttlefish, Sepia esculenta by ammonium sulfate fractionation and column chromatography on Chitin EX, DEAE-Toyopearl 650S, and hydroxyapatite columns. The purified enzyme (SeChi) was identified as a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with an apparent molecular mass of 62 kDa. When pNp-(GlcNAc) 2 was used as a substrate, the optimum pH and optimum temperature for SeChi activity were 3.5 and 50 degrees C, respectively. The activity of SeChi was increased to 164% in the presence of 0.5 M NaCl. Of the insoluble polymer substrates, SeChi exhibited the highest activity on colloidal chitin.
引用
收藏
页码:238 / 243
页数:6
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