Transfer of high-mannose-type oligosaccharides to disaccharides by endo-β- N-acetylglucosaminidase from Arthrobacter protophormiae

Endo-β- N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) has transglycosylation activity, and high-mannose-type oligosaccharides are transferred to suitable glycosides as acceptor substrates. The acceptor specificity of Endo-A-catalyzed transglycosylation toward various disaccharides...

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Published inJournal of bioscience and bioengineering Vol. 93; no. 6; pp. 614 - 617
Main Authors Fujita, Kiyotaka, Miyamura, Tsuyoshi, Sano, Mutsumi, Kato, Ikunoshin, Takegawa, Kaoru
Format Journal Article
LanguageEnglish
Published Amsterdarm Elsevier B.V 2002
Elsevier Science
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Summary:Endo-β- N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) has transglycosylation activity, and high-mannose-type oligosaccharides are transferred to suitable glycosides as acceptor substrates. The acceptor specificity of Endo-A-catalyzed transglycosylation toward various disaccharides was investigated. To identify an effective acceptor for the transglycosylation by Endo-A, the reaction was carried out using various disaccharides. Endo-A transferred high-mannose-type oligosaccharides more efficiently to β-linked disaccharides (cellobiose, gentiobiose, sophorose, and laminaribiose) than to α-linked disaccharides (isomaltose, maltose, nigerose, kojibiose, and trehalose) as acceptor substrates. The transglycosylation products, (Man) 6GlcNAc-Glc-β-Glc, were more rapidly hydrolyzed than (Man) 6GlcNAc-Glc-α-Glc. These results indicate that Endo-A recognizes the anomeric configuration of the acceptor substrates, and β-linked glycosides are suitable for the synthesis of transglycosylation products.
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ISSN:1389-1723
1347-4421
DOI:10.1016/S1389-1723(02)80247-X