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Citation: HE Jin-Xing, LIU Chang-Xian, SUN Xiao-Mei. Enzymatic Kinetics Characterizations of Immobilized Alcohol Dehydrogenase in Reversed Micelle[J]. Chinese Journal of Applied Chemistry, ;2009, 26(8): 981-984. shu

Enzymatic Kinetics Characterizations of Immobilized Alcohol Dehydrogenase in Reversed Micelle

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

Corresponding author: LIU Chang-Xian,
Received Date: 5 August 2008
Available Online: 28 October 2008
Fund Project: 中南民族大学自然科学基金资助项目(YZZ05018) (YZZ05018)

The immobilization of alcohol dehydrogenase(ADH) with cetyl trimethyl ammonium bromide(CTAB)-octane-hexanol reversed micelle system was performed.The effects of w₀([water]/[CTAB]),pH value in enzyme solution,concentrations of CTAB and hexanol on the immobilization of ADH were studied.The result on the kinetic characterizations of the free and immobilized enzyme indicates that optimum pH values for the enzymatic reactions were 8.2 and 8.8,the optimum temperatures were 31 ℃ and 20 ℃,respectively.The K_m values for alcohol were 12 mmol/L and 7.4 mmol/L,respectively.When the enzyme was deposited for 150 min at 30 ℃,the activities were lost by 90% and 50% for the free and the immobilized enzymes respectively,indicating that the immobilized ADH in reversed micelle has a better thermal stability.
- reversed micelles,
- alcohol dehydrogenase,
- immobilization,
- enzymatic kinetics,
- inhibition
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