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영어
The extracellular enzyme produced by Bacillus subtilis subsp. subtilis A-53 isolated from sea-water was purified by ammonium sulfate saturation of supernatant of culture broth after removal of cells and column chromatography through HiTrapTM QXL ion exchange column and Mono Q ion exchange column. The molecular weight of purified enzyme was estimated to be about 56 KDa by sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE).
Carboxymethylcellulose (CMC), xylan, cellobiose, Filter paper, cellulose, avicel and p-nitrophenyl-β-D-glucopyranoside (pNPG) as a substrate for the purified enzyme were tested. Among them, carboxymethylcellulose (CMC) was found to be the best substrate. Optimal temperature and pH for the CMCase were determined to be 50℃and 6.5, respectively. The CMCase was found to be stable between pH 6.0 and pH 9.0. The enzyme retained over 40% of its original activity within the pH 6.0 to 9.0 for 8hr. K+, Ni+ and EDTA increased the
activity of the CMCase, while Co2+, Hg2+ decreased the activity.