Title Purification and Properties of a Membrane-bound Alcohol Dehydrogenase from Acetobacter sp. HA
Author Yoo, Jin Cheol * · Sim, Jung Bo · Kim, Heung Keun¹ · Chun, Hong Sung¹ · Kim, Sung Jun¹
Address Department of Pharmacy; ¹Department of Genetic Engineering Chosun University
Bibliography Korean Journal of Microbiology, 32(1),78-83, 1994
Key Words Acetobacter sp. HA, alcohol dehydrogenase, purification, characterization
Abstract Membrane-bound alcohol dehydrogenase(ADH) was purified to homogeneous state fron an acetic acid producing bacteria, Acetobacter sp. HA. The enzyme was purified about 153-fold with an overall yield of 35% from the crude cell extract by solubilization and extraction of the enzyme with Triton X-100 and subsequent fractions by column chromatography. Upon sodium dodecyl sulphate-PAGE, the enzyme showed the presence of three subunits with a molecular mass of 79,000 daltons, 49,000, and 45,000 daltons, respectively. Absorption oxidized aliphatic alcohols with a straight carbon chain except for methanol. Formaldehyde, acetaldehyde and glutaraldehyde were also oxidizable substrates. The apparent K_m for ethanol was 1.38mM. The optimun pH and temperature were 5.0~6.0 and 32℃, respectively. V_2O_5 and heavy metals such as ZnCl_2 and NiCl_2 were inhibitory to the enzyme activity.
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