Abstract
Laccase from Coriolus versicolor and bilirubin oxidases from Trachyderma tsunodae and Myrothecium verrucaria converted 4-hydroxymandelic acid (HMA) and 2-(4-hydroxyphenyl)glycine into 4-hydroxybenzaldehyde (HBA), which was a single product and was not converted further. The reactions were oxidative decarboxylations that were considered to be caused by the enzyme-catalyzed abstractions of hydrogen from the phenolic hydroxyl groups. The decarboxylation of HMA was used for a new colorimetric measurement of the activities of these enzymes. One unit of the enzymes was defined as the amount that catalyzed the formation of 1 μmol of HBA per minute. When HMA was used for a substrate, the optimum pHs of laccase, bilirubin oxidase from T. tsunodae, and bilirubin oxidase from M. verrucaria were 4.5, 5.0, and 8.5, respectively, and their Km values were 31.3 mM, 34.5 mM, and 22.3 mM, respectively.
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