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

Biochemistry (Mosc). 2007 Jan;72(1):29-36. doi: 10.1134/s0006297907010038.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antiviral Agents / chemistry
  • Glucan 1,3-beta-Glucosidase / metabolism*
  • Glucans / chemistry*
  • Glucans / metabolism
  • Hydrolysis
  • Magnetic Resonance Spectroscopy
  • Oligosaccharides / chemistry
  • Spisula / enzymology*
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Antiviral Agents
  • Glucans
  • Oligosaccharides
  • epiglucan
  • Glucan 1,3-beta-Glucosidase