Abstract
The oxidation of methanol by the enzyme methanol oxidase leads to the formation of formaldehyde and hydrogen peroxide. However, methanol oxidase from the yeast Hansenula polymorpha is heavily contaminated with catalase which leads to the decomposition of the hydrogen peroxide. To eliminate the catalase activity, partial purification through gel chromatography followed by a simple selective temperature inactivation has proven to be very successful. Hydrogen peroxide, unfortunately, readily inactivates methanol oxidase. To overcome this problem, in situ extraction of hydrogen peroxide during enzymatic reaction was examined. The best solvent was quinoline which was studied using soluble and polyacrylamide entrapped enzyme systems.
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