Enzymatic Synthesis of 2-Chloro-4-nitrophenyl 4,6-O-3-Ketobutylideneβ-Maltopentaoside, a Substrate forα-Amylase

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Abstract
A transglycosylation reaction with 2-chloro-4-nitrophenyl beta-maltoside as an acceptor was done with 4,6-O-3-ketobutylidene maltopentaose and Bacillus macerans cyclodextrin glucanotransferase in an aqueous solution containing 50% n-propanol, and there were two main transglycosylation products. They were identified as 2-chloro-4-nitrophenyl 4,6-O-3-ketobutylidene beta-maltopentaoside and 2-chloro-4-nitrophenyl 4,6-O-3-ketobutylidene beta-maltohexaoside, and their yields were 30% and 21% respectively on the basis of the decrease of 4,6-O-3-ketobutylidene maltopentaose. For the production of 2-chloro-4-nitrophenyl 4,6-O-3-ketobutylidene beta-maltopentaoside at high substrates concentrations, the addition of n-propanol in this reaction not only increased the solubility of 2-chloro-4-nitrophenyl beta-maltoside sufficiently but also suppressed side reactions.

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