十二烷基磺酸钠所致外切葡聚糖纤维二糖水解酶底物专一性的变化

Changes of specificity of cellobiohydrolase I caused by the treatment of sodium dodecyl sulfate

以低浓度的十二烷基磺酸钠(SDS)为微扰剂处理外切葡聚糖纤维二糖水解酶（CBHI），由荧光、圆二和二阶导致话测定反应动力学常数。结果表明低浓度的SDS处理可显著增加CBHI的内切酶活力，推测是CBHI活性位点附近的色氨酸所处微环境发生了变化，影响了酶与纤维素的结合所致。对近年来在分子水平上研究纤维素酶废物专一性的结果作了评述。

Active changes of ce1lobiohydrolase I (CBH I), caused by the treatment of sodium dodecyl sulfate SDS, was investigated. Kinetic analysis was determined by the methods offluorescence and circu1ar dichronism. The treatment of SDS under low concentration can increasesthe endoglucanase activity of CBH I. This result may be explained that treatment of SDS cancaused the changes of micro - environment of trytophan clase1y in active center of CBH I, and soeffects the combination between enzyme and substrate