Enzymatic synthesis of p-nitrophenyl 35-O-β-N-acetylglucosaminyl-α-maltopentaoside by lysozyme ; a novel substrate for human amylase assay
Enzymatic synthesis of p-nitrophenyl 35-O-β-N-acetylglucosaminyl-α-maltopentaoside by lysozyme ; a novel substrate for human amylase assay
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溶菌酶酶法合成对硝基苯基 35-O-β-N-乙酰氨基葡萄糖-α-麦芽五糖苷；一种用于人淀粉酶测定的新型底物；
DOI：
10.1016/0304-4165(90)90178-y
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
T. Usui
中科院分区：
文献类型：
--
作者：
H. Matsui;H. Kawagishi;T. Usui
用鸡蛋清溶菌酶区域选择性地诱导二-N-乙酰壳二糖转糖到对硝基苯基α-麦芽五糖苷非还原性末端葡萄糖基3-位。该酶以二-N-乙酰基壳二糖为供体，对硝基苯基α-麦芽五糖苷为受体，生成对硝基苯基35-O-β-N-乙酰氨基葡萄糖基-α-麦芽五糖苷（占酶催化的对硝基苯基α-麦芽五糖苷净减少量的5%）。转糖基化反应的速率与底物浓度、温度和pH有关。麦芽五糖苷衍生物可作为α-淀粉酶的底物，通过α-D-葡萄糖苷酶和葡萄糖淀粉酶的偶联反应进行测定。
Transglycosylation from di-N-acetylchitobiose to the 3-position at the nonreducing end glucosyl group ofp-nitrophenyl α-maltopentaoside was regioselectively induced through the use of hen egg-white lysozome. The enzyme formedp-nitrophenyl 35-O-β-N-acetylglucosaminyl-α-maltopentaoside (5% of the enzyme-catalyzed net decreased ofp-nitrophenyl α-maltopentaoside) from di-N-acetylchitobiose as a donor andp-nitrophenyl α-maltopentaoside as an acceptor. The rate of the transglycosylation depended on the concentration of substrate, the temperature and the pH. The hydrolytic actions of human pancreatic and salivary α-amylase on this derivative were examined. The maltopentaoside derivative was shown to be useful as a substrate for α-amylase assay through a coupled reaction involving α-D-glucosidase and glucoamylase.