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A microsomal membrane bound alcohol oxidase enzyme was isolated from a hydrocarbon degrading Aspergillus terreus fungus that could oxidize short chain,long chain, secondary, and arylalcohol substrates. High aggregating property of the protein was demonstrated by AFM, DLS and TEM analyses. Chemical analysis showed the presence of oleic acid and palmitic acid at a ratio of 2:1 in the purified protein. We have demonstrated a highly efficient method for dissociation and simultaneous deflavination of the alcohol oxidase protein using ?ME. The potential applications of this approach on preparing apoprotein and its reassemble with FAD to a functional enzyme are envisaged in the preparation of enzyme electrodes for biosensor and biofuel cell applications. The findings obtained through this investigation have revealed many interesting facts about this novel microsomal alcohol oxidase enzyme.This investigation has opened up new avenue on the research to explore the architecture of alcohol oxidase proteins from fungal sources including their structurefunction relationship and potential applications.
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birth defects, or other reproductive harm.
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