Chinese Journal of Applied Chemistry ›› 2009, Vol. 26 ›› Issue (08): 981-984.

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Enzymatic Kinetics Characterizations of the Immobilized Alcohol Dehydrogenase in Reversed Micelles

HE Jin-Xing, LIU Chang-Xian*, SUN Xiao-Mei   

  1. (Key Laboratory for Analytical Chemistry of the State Ethnic Affairs Commission,College of
    Chemistry and Material Science,South-Central University for Nationalities,Wuhan 430074)
  • Received:2008-08-04 Revised:2008-10-09 Published:2009-08-10 Online:2009-08-10

Abstract:

The immobilization for alcohol dehydrogenase(ADH) with cetyl trimethyl ammonium bromide(CTAB)-octane-hexanol reversed micelles system was introduced.The effect for the immobilization of the w0(=[water]/[CTAB]),the pH value in enzyme solution,the concentration of CTAB and hexanol were assayed.The study on the kinetic characterizations of the free and immobilized enzyme indicates that optimum pH value of the enzymatic reaction were 8.2 and 8.8, the optimum temperature were 31℃ and 20℃ respectively. The Km value for alcohol were 12mmol/L and 7.4mmol/L respectively. The enzymes were deposited for 150min at 30℃, the activities were lost 90% and 50% for the free enzyme and the immobilized enzyme respectively. It indicates that the immobilized ADH in reversed micelles has better thermal stability.

Key words: reversed micelles, alcohol dehydrogenase, immobilization, enzymatic kinetics, inhibition

CLC Number: