Enzymatic Synthesis of p-Nitrophenyl α-Maltoheptaoside by Transglycosylation of Maltohexaose-forming Amylase(Biological Chemistry)
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概要
- 論文の詳細を見る
An extracellular maltohexaose-forming amylase [EC 3.2.1.98] from Klebsiella pneumoniae mutant is a normal hydrolytic enzyme that hydrolyzes short-chain amylose (<DP>^^^- = 23) to give about 40% maltohexaose. Transglycosylation from maltoheptaose to the 4-position of p-nitrophenyl α-glucoside was efficiently induced through the use of maltohexaose-forming amylase in an aqueous methanol solution. The enzyme specifically produced p-nitrophenyl α-maltoheptaoside (13% of the p-nitrophenyl α-glucoside) from maltoheptaose as a donor and p-nitrophenyl α-glucoside as an acceptor. The yield of p-nitrophenyl α-maltoheptaoside depended on the concentration of methanol solvent, the pH, and temperature. Furthermore, the use of the aqueous methanol system in the reaction not only improved the solubility of p-nitrophenyl α-glucoside but also greatly increased the formation of p-nitrophenyl α-maltoheptaoside, which is a useful substrate for assay of human amylase in serum and urine.
- 社団法人日本農芸化学会の論文
- 1990-03-23
著者
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Usui Taichi
Department Of Agricultural Chemistry Faculty Of Agriculture Shizuoka University
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OGAWA Koichi
Research Center for Frontier Medical Engineering, Chiba University
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Nakakuki Teruo
Research Institute, Nihon Shokuhin Kako Co., Ltd.
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Kainuma Keiji
Biotechnology Division Ministry Of Agriculture Forestry And Fisheries
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Uejima Osamu
Research Laboratory Nibon Shokuhin Kako Co. Ltd.
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Ogawa Koichi
Research Center For Frontier Medical Engineering Chiba University:communication Devices Development
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Nakakuki Teruo
Research Laboratory Nibon Shokuhin Kako Co. Ltd.
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Nakakuki Teruo
Research Institute Nihon Shokuhin Kako Co. Ltd.
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Ogawa Koichi
Research Laboratory Nibon Shokuhin Kako Co. Ltd.
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