Environmentally benign glycosylation of aryl pyranosides and aryl/alkyl furanosides demonstrating the versatility of thermostable CGTase from Thermoanaerobacterium sp.
Literature Information
Luis Herrera-Estrella, Anne-Laure Chauvin
An extensive study on the specificity of transglycosylation and disproportionation of Thermoanaerobacterium sp. cyclodextrin glucosyltransferases against aryl glucopyranosides or furanosides is reported. While a mixture of maltoside and isomaltoside was obtained respectively using p-nitrophenyl glucopyranoside as an acceptor, only one regioisomer, namely p-nitrophenyl α-D-Glcp-(1,3)-α-L-Araf, was isolated using p-nitrophenyl arabinofuranoside as an acceptor. Interestingly, similar outcomes were found when using p-nitrophenyl galactofuranoside. Furthermore, activation by microwave irradiation resulted in faster reaction times and higher yields and led to glucosidic oligosaccharides with up to 70% conversion. The influence of the anomeric and C-4 configurations of the glycosidic acceptors on the transglycosylation, previously stated for the CGTase family, was not observed and unconventional substrate specificity towards alkyl furanosides was highlighted.
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