Abstract
Polyphenol oxidase from Granny Smith apples was purified and characterized in both its soluble form (sPPO) and its membrane-bound form (mPPO). Both forms were purified by temperature-induced phase partitioning, precipitation with ammonium sulfate, and ion exchange chromatography. The specific activity of mPPO was 19.17 times that of sPPO. The optimum pH and temperature for both forms were 7.0 and 35 °C when catechol was the substrate. The Michaelis constant and maximum reaction rate for sPPO were 34.1 mM and 500 U/mL/min, whereas those for mPPO were 53 mM and 10,000 U/mL/min, respectively. The enzymes exhibited diphenolase activity, and their affinity was highest for catechol (sPPO) and 4-methylcatechol (mPPO). Inhibitors of sPPO and mPPO included ascorbic acid, glutathione, and l-cysteine. However, ethylenediaminetetraacetic acid increased the activity of mPPO. Purified sPPO was dimeric with a molecular weight of 31 kDa, whereas mPPO was monomeric with an estimated molecular weight of 65 kDa.
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