Abstract
Glycerol oxidase is a novel enzyme that catalyzes the oxidation of glycerol in the presence of oxygen to glyceraldehyde and hydrogen peroxide without the requirement of any exogenous cofactors. The enzyme is formed in some strains of Aspergillus, Neurospora , and Penicillium, grown on glycerol as a sole carbon source. Protoheme IX and copper ions are contained in the enzyme as prosthetic groups. The enzyme, in combination with lipoprotein lipase, is employed in a spectrophotometric assay for triglycerides in sera. This chapter describes the assay method of glycerol oxidase isolated from Aspergillus japonicas . The enzyme assay is based on the measurement of hydrogen peroxide generated in the oxidation of glycerol. The hydrogen peroxide is oxidized with 4-aminoantipyrine and phenol in the presence of peroxidase to form a quinoneimine dye. The steps involved in the purification procedure of glycerol oxidase are also discussed in the chapter. The purified enzyme sediments as a single, symmetric schlieren peak on ultracentrifugation and gives a single band on acrylamide gel electrophoresis at pH 8.3.
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