Abstract
A continuous spectrophotometric method for the determination of the monophenolase and diphenolase activities of apple polyphenol oxidase is described. The method is based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid and 3,4-dihydroxyphenyl propionic acid in the presence of polyphenol oxidase. The λ max and the molar absorptivity (ϵ) for the MBTH-quinone adduct have been calculated. The presence of MBTH in the reaction medium decreases the lag period during the expression of monophenolase activity. The high value of V max suggests the existence of a high catalytic constant. This, together with the value of ϵ for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods.
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