Comparison of the Enzymatic Activities of Endo-1,4-.BETA.-Glucanases Derived from Clostridium josui.

Accession number;00A0559774
Title;Comparison of the Enzymatic Activities of Endo-1,4-.BETA.-Glucanases Derived from Clostridium josui.
Author; FUJINO E (Mie Univ., Mie) FUJINO T (Nagoya Seiraku Co. Ltd., Aichi) SAKKA K (Mie Univ., Mie) KIMURA K (Mie Univ., Mie) OHMIYA K (Mie Univ., Mie)
Journal Title;Bull Fac Bioresour Mie Univ
Journal Code:Y0251B
ISSN:0915-0471
VOL.;NO.23;PAGE.23-30(1999)
Figure&Table&Reference;FIG.2, TBL.3, REF.21
Pub. Country;Japan
Language;English
Abstract;Endoglucanase EG-1C, -2C and -3 (EC 3.2.1.4) derived from C. josui were highly active in degrading of carboxymethyl cellulose (CMC), but only slightly active on Avicel. All enzymes could not hydrolyze xylan and p-Nitrophenyl-.BETA.-D-glucoside. p-Nitrophenyl-.BETA.-D-cellobioside was degraded only by EG-1C. By CMC and cellooligosaccharide degrading analysis, the specific activity of EG-2C against CMC was 5 times higher than the others and its action mode was most endowisely. In degrading cello-oligosaccharides, these enzymes could degrade cellotetraose and cellopentaose, but not cellobiose and cellotriose. The specific activities increased as degree of polymerization increases from four to five. (author abst.)