Specificity of 1,3-β-glucanases from the lytic system of Streptomyces sp. 1228

• Published in: Biotechnology letters Vol. 11; no. 4; pp. 287 - 292
• Main Authors: BIELECKI, S, ANTCZAK, T, WNUK, M, BOBOWICZ-LASSOCINSKA, T, GALAS, E
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01-04-1989
• Subjects: Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Fundamental and applied biological sciences. Psychology; Growth, nutrition, metabolism, transports, enzymes. Molecular biology; Microbiology; Mission oriented research; Mycology; oligosaccharides; Physiology and metabolism; polysaccharides; Streptomyces; Streptomycetaceae; Yeast; Enzyme; Isozyme; Cellulose; Streptomyces; Xylan; Actinomycetales; Glucan; Enzymatic activity; Substrate specificity; Bacteria; Actinomycetes; Carbohydrate; Glucanase
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1007/BF01031579

Four 1,3- beta -glucanases GI, GII, GIV and GVIII, which were isolated from culture filtrate of Streptomyces sp. 1228, were examined for their activities on different oligo- and polysaccharides containing 1,3- beta - and/or 1,4- beta - and/or 1,6- beta -glycosodic bonds. Linear 1,3- beta -glucan - laminarin was extensively degraded. CM-cellulose, xylan, lichenan and yeast glucan were hydrolyzed to different extents by the four enzymes. No activity against barley glucan was found. Laminarioligosaccharides, with a higher degree of polymerization were more extensively hydrolyzed by GI, GII, and GIV enzymes. Glucanase GVIII prefers substrates with lower molecular mass.