Abstract
A β-1, 3-glucanase was obtained from culture filtrate of C. rolfsii by precipitation with ammonium sulfate and purified by DEAE-cellulose chromatography and Sephadex G-100 gel-filtration. The purification gave a 34.5-fold increase in specific activity. The enzyme was stable over the pH range 2.0_??_9.0, and retained 74% of its activity when stored at pH 2.0 and 5°C for 72 hr; maximum activity occured at pH 4.5 and 55°C; the inhibitory effect of Hg2+ or Fe2+ was observed. In the initial reaction, glucose was produced from laminarin at high reaction rate; 80μg per min per μg of enzyme protein at pH 4.5 and 40°C. The reaction product was determined by paper chromatography to be largely glucose after 5min_??_72 hr incubation, but oligosaccharides were also detected as faint spots after 5_??_72 hr incubation.
