Abstract
ABSTRACT A maltopentaose-forming amylase [EC 3.2.1.1] from Bacillus licheniformis effectively produced p-nitrophenyl α-maltohexaoside (3) through a transglycosylation reaction from maltohexaose as a donor and p-nitrophenyl α-glucoside (1) as an acceptor in an aqueous solution containing hydrophilic organic solvents. The enzyme specifically transferred from maltohexaose to the 4-position of 1. The yield of 3 depended on the kind of donor, concentration of solvent, pH, and temperature. By the addition of solvents such as dimethyl sulfoxide and 1-butanol, respectively, effects of acceleration on transferase activity of the enzyme and improvement of acceptor solubility were achieved, and resulted in a great increase in the formation of 3.
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