Purification and Some Properties ofβ-1,3-Glucanase fromStreptomycessp.

Publisher Website
Google Scholar
Abstract
β-1,3-Glucanase was purified from the culture filtrate of a Streptomyces sp. by ammonium sulfate fractionation, hydroxylapatite and DE-52 column chromatographies, gel filtration on Biogel P-100 and isoelectric focusing. The purified β-1,3-glucanase was homogeneous on polyacrylamide disc-gel electrophoresis. The isoelectric point was pH 3.7, and the molecular weight was 36,000. The optimum pH and temperature for the activity of the enzyme were 5.5 and 55°C, respectively. The enzyme was stabilized by Ca2+, but inactivated by Hg2+, and was inhibited by N-bromo-succinimide. The glucanase did not hydrolyze laminaribiose or sophorose, cellobiose, or gentio-biose. The enzyme ultimately hydrolyzed laminari-oligosaccharides (laminaritriose to laminarihexaose) to glucose and laminaribiose, and their sugar alcohols (laminaritriitol to laminarihexaitol) mainly to laminaribiose and laminaribiitol via a disproportionation reaction.