Chemistry of Natural Compounds

, Volume 18, Issue 3, pp 261–267 | Cite as

Characteristics of a β-1,3-glucanase fromSpisula sachalinensis as a glycoprotein

  • O. M. Myastovskaya
  • V. V. Sova
  • L. A. Elyakova
Article
  • 26 Downloads

Abstract

The nature of the carbohydrate-peptide bond and the composition of the carbohydrate chain in a β-1,3-glucanase from the marine molluskS. sachalinensis has been investigated. According to the results of the phenol-sulfuric acid method, the neutral sugars amounted to 6.5% of the molecular weight of the enzyme. The composition of the neutral sugars (Glc : Gal : Man 5:2:1) was determined by the GLC method. It was shown that the β-1,3-glucanase molecule contains no uronic or sialic acids. The amount of amino sugars (15% with equal amounts of glucosamine and galactosamine) was established by amino acid analysis. Alkaline degradation led via the β-elimination reaction to the splitting out of 50% of the neutral sugars and showed the existence of an O-glycosidic bond in the enzyme molecule. Various actions on the carbohydrate moiety (periodate oxidation and treatment with glycosidases) caused no appreciable change in the hydrolyzing capacity of the enzyme.

Keywords

Sialic Acid Amino Sugar Neutral Sugar Cyclooctene Marine Mollusk 

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Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

  • O. M. Myastovskaya
  • V. V. Sova
  • L. A. Elyakova

There are no affiliations available

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