Enzymatic glycosylation of indoxyglycosides catalyzed by a novel maltose phosphorylase from Emticicia oligotrophica. Issue 6 (23rd July 2016)

• Record Type: Journal Article
• Authors: Awad, Faisal Nureldin; Kulinich, Anna; Yao, Ming Jun; Duan, Xu Chu; Cai, Zhi Peng; Gu, Bin; Liu, Li; Voglmeir, Josef
• Is Part Of: Journal of carbohydrate chemistry. Volume 35:Issue 6(2016)
• Page Start: 301
• Page End: 314
• Publication Date: 2016-07-23
• Subjects: X-glycosides -- Emticicia oligotrophica -- maltose phosphorylase -- maltose -- phosphorolysis -- beta glucose 1 phosphate; Carbohydrates -- Periodicals; 547.78
• DOI: 10.1080/07328303.2016.1238479
• Languages: English
• ISSNs: 0732-8303

Abstract

GRAPHICAL ABSTRACT: ABSTRACT: Maltose phosphorylases (EC 2.4.1.8) catalyze the reversible conversion of maltose to glucose and glucose-1-phosphate in the presence of inorganic phosphate. Herein, we describe for the first time the use of a maltose phosphorylase for the synthesis of various anomerically modified diglycosides. The maltose phosphorylase used was isolated from the bacterium Emticicia oligotrophica and showed a high selectivity towards the phosphorolysis of maltose, whereas no phosphorolysis was observed using other glucose-containing disaccharides such as cellobiose, melibiose, sucrose and trehalose. The addition of glucose to various 5-bromo-4-chloro-3-indolyl-glycosides (X-sugars) was used to evaluate the promiscuity of the maltose phosphorylase, and product formation was verified by LC-ESI-MS and MALDI-TOF-MS. The simple expression and purification protocol and the use of maltose as an inexpensive starting material make this maltose phosphorylase from Emticicia oligotrophica a valuable novel biocatalyst for the synthesis of glucose-containing glycosides.