The enzymatic kinetics of immobilized lactate dehydrogenase( LDH) and alcohol dehydrogenase( ADH) with cetyl trimthyl ammonium chloride( CTAC)-pentanol-octane reversed micelle system were investigated. The effect of the level of water,the concen-tration of surfactant and cosolvent on the immobilization of LDH and ADH were assayed. The enzymatic characterizations of free and immobilized enzymes were also studied. In the case of LDH,the optimum pH of enzymatic reaction were 9. 2 and 9. 0 for the free and immobilized ones,respectively the optimum temperature were 51℃ and 29℃,respectively the michaelis constant were 15mmol ·L-1 and 2mmol·L-1 ,respectively. With regard to ADH,the optimum pH of enzymatic reaction were 8. 8 and 8. 2 for the free and immobilized ones,respectively the optimum temperature were 33℃ and 39℃,respectively the michaelis constant were 4mmol·L-1 and 17mmol·L-1 ,respectively. The immobilized enzymes could be used to determine trace component in samples.%探讨十六烷基三甲基氯化铵( CATC )-戊醇-辛烷反胶束体系固定化乳酸脱氢酶( LDH )和醇脱氢酶( ADH)的催化作用。试验了含水量、表面活性剂以及助溶剂浓度对于酶固载量的影响。对游离酶和固定化酶催化性质研究表明：LDH酶促反应的适宜 pH值分别为9．2和9．0,适宜温度为51℃和29℃,米氏常数15mmol·L-1和2mmol·L-1；ADH 酶促反应的适宜 pH 值为8．8和8．2,适宜温度为33℃和39℃,米氏常数4mmol·L-1和17mmol·L-1。应用反胶束固定化酶测定了试样中微量组分。
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