Enzymatic synthesis of p-nitrophenyl alpha-maltopentaoside in an aqueous-methanol solvent system by maltotetraose-forming amylase: a substrate for human amylase in serum.
Enzymatic synthesis of p-nitrophenyl alpha-maltopentaoside in an aqueous-methanol solvent system by maltotetraose-forming amylase: a substrate for human amylase in serum.
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通过形成麦芽四糖的淀粉酶在水-甲醇溶剂系统中酶促合成对硝基苯基α-麦芽五糖苷：血清中人淀粉酶的底物。
DOI：
10.1093/oxfordjournals.jbchem.a122395
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发表时间：
1988
影响因子：
2.7
通讯作者：
T. Murata
中科院分区：
文献类型：
--
作者：
T. Usui;T. Murata
在含有高浓度甲醇的水溶液中，利用斯氏假单胞菌产生麦芽四糖的淀粉酶，可以有效地诱导麦芽五糖到对硝基苯基α-葡萄糖苷4位的糖基化反应。该酶以麦芽五糖为供体，以对-硝基苯基-α-葡萄糖苷为受体，特异地合成了对-硝基苯基-α-麦芽五糖苷(占酶促麦芽五糖净减少量的12%)。糖基化反应的速率与甲醇浓度、pH和温度有关。在该反应中采用甲醇水相体系，不仅保证了对硝基苯基α-葡萄糖苷的充分溶解，而且显著增加了测定血清和尿液中人淀粉酶的底物对硝基苯基α-麦芽五醇苷的生成。
Transglycosylation from maltopentaose to the 4-position of p-nitrophenyl alpha-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 alpha-maltopentaoside (12% of the enzyme-catalyzed net decrease of maltopentaose) from maltopentaose as a donor and p-nitrophenyl alpha-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 alpha-glucoside but also resulted in a remarkable increase in the formation of p-nitrophenyl alpha-maltopentaoside, which is a useful substrate for assay of human amylase in serum and urine.