Enzymatic Transformation of Biologically Active 1,3;1,6-beta-D-Glucan. Structure and Activity of Resulting Fragments

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L. A. Elyakova, V. V. Isakov, L. A. Lapshina, V. P. Nagorskaya, G. N. Likhatskaya, T. N. Zvyagintseva^*, and A. V. Reunov

Pacific Institute of Bioorganic Chemistry, Far East Division, Russian Academy of Sciences, pr. 100-letiya Vladivostoka 159, 690022 Vladivostok, Russia; fax: (4232) 31-4050; E-mail: zvyag@piboc.dvo.ru

^* To whom correspondence should be addressed.

Received January 12, 2006; Revision received July 19, 2006

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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.

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KEY WORDS: biologically active 1,3;1,6-beta-D-glucan, 1,3-beta-D-glucanase, marine mollusks, enzymatic transformation, tobacco mosaic virus, anti-viral activity, stabilizing action on membranes

DOI: 10.1134/S0006297907010038

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