Abstract
Purification of blueberry polyphenol oxidase (PPO) has not been substantially progressed for a long time, which leads to little further study. We purified three PPOs from blueberries for the first time by modified Native-Page. The PPO-2 consists of two subunits (68 and 36 kDa), whereas PPO-3 and PPO-4 contain only one subunit (36 kDa). The optimum pH and temperature of PPO-2, PPO-3, and PPO-4 were 5.8–6.2 and 40 °C–45 °C with catechol as a substrate. The optimal substrates for them were all catechol (Km = 14.91, 7.19, and 11.20, respectively). High-pressure processing (HPP) had a limited inhibitory effect on the three PPOs. The activities of PPO-2, PPO-3, and PPO-4 were significantly reduced with increased SDS concentration. The binding of substrate to catalytic cavity is related to the residues His76, His209, His213, Gly228, and Phe230. The carbonyl group of residue Gly228 is one of the key sites for screening substrates.
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