The release of oligosaccharides from glycoproteins by endo-β-N-acetylglucosaminidase of Flavobacterium sp.

Kenji Yamamoto, Kauro Takegawa, Jianqiang Fan, Hidehiko Kumagal, Tatsurokuro Taochikura

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Endo-β-N-acetylglucosaminidase, purified to homogenicity from the cultural filtrate of Flavobacterium sp., liberated oligosaccharides from various glycoproteins. The enzyme could liberate the carbohydrate chain from native ovalbumin. The release of oligosaccharides from ribonuclease B, yeast carboxypeptidase and a Ricinus lectin was also observed. These glycoproteins contain neutral oligosaccharides that are attached to the protein through glycosyl asparagine bonds. The treatment of glycoprotein with SDS and boiling was more effective for removal of oligosaccharides by the enzyme. The enzyme hydrolyzed all five heterogeneous ovalbumin glycopeptides, although the rate of hydrolysis decreased as the size of the sugar moiety increased. Removal of the neutral oligosaccharides did not appear to effect the enzymatic properties of the hemagglutination ability of these glycoproteins.

Original languageEnglish
Pages (from-to)397-403
Number of pages7
JournalJournal of Fermentation Technology
Volume64
Issue number5
DOIs
Publication statusPublished - Jan 1 1986
Externally publishedYes

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