Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Enzymatic Synthesis of 2-Chloro-4-nitrophenyl 4, 6-O-3-Ketobutylidene β-Maltopentaoside, a Substrate for α-Amylase
Katsutoshi ISHIMARUYoshikazu KAMEZONOShinichi TESHIMAYuzo HAYASHI
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1992 Volume 56 Issue 10 Pages 1552-1556

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Abstract
A transglycosylation reaction with 2-chloro-4-nitrophenyl β-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 β-maltopentaoside and 2-chloro-4-nitrophenyl 4, 6-O-3-ketobutylidene β-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 β-maltopentaoside at high substrates concentrations, the addition of n-propanol in this reaction not noly increased the solubility of 2-chloro-4-nitrophenyl β-maltoside sufficiently but also suppressed side reactions.
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