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 aryl-alcohol 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 β-ME. The potential applications of this approach on...
A microsomal membrane bound alcohol oxidase enzyme was isolated from a hydrocarbon degrading Aspergillus terreus fungus that could oxidize short chain...