Enzymatic transformation of biologically active 1,3;1,6-beta-D-glucan. Structure and activity of resulting fragments

• Published in: Biochemistry (Moscow) Vol. 72; no. 1; pp. 29 - 36
• Main Authors: Elyakova, L A, Isakov, V V, Lapshina, L A, Nagorskaya, V P, Likhatskaya, G N, Zvyagintseva, T N, Reunov, A V
• Format: Journal Article
• Language: English
• Published: United States 01.01.2007
• Subjects: Animals; Antiviral Agents - chemistry; Glucan 1,3-beta-Glucosidase - metabolism; Glucans - chemistry; Glucans - metabolism; Hydrolysis; Magnetic Resonance Spectroscopy; Mollusca; Oligosaccharides - chemistry; Spisula - enzymology; Spisula sachalinensis; Structure-Activity Relationship; Substrate Specificity; Tobacco mosaic virus
• ISSN: 0006-2979; 1608-3040; 0320-9725
• DOI: 10.1134/S0006297907010038

The fragmentation of the biologically active 1,3;1,6-beta-D-glucan Antivir by endo-1,3-beta-D-glucanase LIV from crystalline styles of the marine mollusk Spisula sachalinensis was carried out. It was found that low molecular mass oligomers possessing a stabilizing effect on membranes and anti-viral activity against tobacco mosaic virus appeared in the process of enzymatic hydrolysis of Antivir. Biological activity of 1,3;1,6-beta-D-glucooligo- and polysaccharides was found to be associated with molecular mass (polymerization degree (n) not less than 14) and with presence of intralinked beta-1,6-connected monosaccharide residues. Probably, decrease in molecular mass is compensated by increase in number of intralinked beta-1,6-connected monosaccharide residues.