Abstract
Pear polyphenol oxidase (PPO) has been isolated by using two sequential phase partitionings with Triton X-114 (TX-114). The enzyme showed monophenolase activity when assayed on p-hydroxyphenyl propionic acid (PHPPA) with 3-methyl-2-benzothiazolinone hydrazone (MBTH) in a continuous spectrophotometric method, with high sensitivity and precision. The initial monophenolase activity showed a lag period (τ) prior to the attainment of the steady state rate ( V ss ). Both kinetic parameters, V ss and τ, depended on the enzyme and monophenol concentrations, as well as on the presence of catalytic amounts of o-diphenol. The enzyme showed an optimum pH of 4.3 and the value of K m toward PHPPA was 0.5 mM.
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