Enzymatic Synthesis of p-Nitrophenyl α-Maltopentaoside in an Aqueous-Methanol Solvent System by Maltotetraose-Forming Amylase: A Substrate for Human Amylase in Serum

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Abstract
Transglycosylation from maltopentaose to the 4-position of p-nitrophenyl α-glucoside was efficiently induced through the use of maltotetraose-forming amylase from Pseudomonas stutzeri in an aqueous solution containing methanol at a high concentration. The enzyme specifically formed p-nitrophenyl α-maltopentaoside (12% of the enzyme-catalyzed net decrease of maltopentaose) from maltopentaose as a donor and p-nitrophenyl α-glucoside as an acceptor. The rate of the transglycosylation depended on the concentration of methanol solvent, the pH and the temperature. Use of the aqueous methanol system in this reaction not only ensured a sufficient solubility of p-nitrophenyl α-glucoside but also resulted in a remarkable increase in the formation of p-nitrophenyl α-maltopentaoside, which is a useful substrate for assay of human amylase in serum and urine.

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