Kinetic studies of dextransucrase enzyme reactions on a substrate- or enzyme-immobilized 27 MHz quartz crystal microbalance.
Kinetic studies of dextransucrase enzyme reactions on a substrate- or enzyme-immobilized 27 MHz quartz crystal microbalance.
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DOI：
10.1021/la104550m
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发表时间：
2011-01
期刊：
影响因子：
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通讯作者：
T. Nihira;Toshiaki Mori;Megumi Asakura;Y. Okahata
中科院分区：
文献类型：
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作者：
T. Nihira;Toshiaki Mori;Megumi Asakura;Y. Okahata
在固定化的27 MHz石英晶体微天平（QCM）上直接监测右旋蔗糖酶（DSase）的催化延伸。测定了酶与葡聚糖受体结合的动力学参数（k（on）、k（off）和k(d)）以及在蔗糖单体存在下酶的延伸(k（m)用于蔗糖和k(cat)）。两种方法得到的动力学参数一致。
Catalytic elongation by dextransucrase (DSase) was monitored directly on a dextran-acceptor- or DSase-immobilized 27 MHz quartz crystal microbalance (QCM). Kinetic parameters for the binding of the enzyme to the dextran acceptor (k(on), k(off), and K(d)) and enzymatic elongation in the presence of a sucrose monomer (K(m) for sucrose and k(cat)) were determined. The kinetic parameters obtained by both methods were consistent.