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  • Title: Comparison of the biochemical properties and thermal inactivation of polyphenol oxidase from three lily bulb cultivars.
    Author: Wang X, Yang L, Liu J, Wang R, Zhang Q, Shan Y, Ding S.
    Journal: J Food Biochem; 2020 Oct; 44(10):e13431. PubMed ID: 33090543.
    Abstract:
    The biochemical properties and thermal inactivation of polyphenol oxidase (PPO) from three main planted lily cultivars in China, namely, Lilium lancifolium Thunb, Lilium brownie var. viridulum, and Lilium davidii var. unicolor cotton were evaluated. Data indicate that the PPO from three cultivars showed two optimum pH levels of 4.0 and 6.5-7.0 and temperature of 15°C and exhibited the highest affinity toward 4-methylcatechol. However, this enzyme did not exhibit monophenolase activity. Thiourea and L-cysteine were more effective than other inhibitors. The enzymatic activity of L. lancifolium Thunb PPO crude extract was higher than that of L. brownie var. viridulum and L. davidii var. unicolor cotton. For thermal inactivation, L. davidii var. unicolor cotton PPO showed the best thermal resistance at 65-75°C, and L. lancifolium Thunb showed stability at 45°C. The deactivation of the three types of PPO followed the first-order reaction kinetics, and the activation energy (Ea) was 144.28, 138.00, and 107.12 kJ/mol for L. lancifolium Thunb PPO, L. brownie var. viridulum PPO, and L. davidii var. unicolor cotton PPO, respectively. PRACTICAL APPLICATIONS: Lilium is an ornamental and edible plant typically used for food and traditional Chinese medicine. Its flowers are used for decoration, and its underground bulbs are rich in various bioactive substances. Fresh lily bulbs easily turn brown and lose economic value during storage and processing. Polyphenol oxidase (PPO) is a crucial molecule involved in the enzymatic browning of fruit and vegetables. In this study, PPO was extracted from three main planted lily cultivars in China. Namely, Lilium lancifolium Thunb, Lilium brownie var. viridulum, Lilium davidii var. unicolor cotton and was partially characterized. The results are of considerable importance to further understand the PPO of lily bulbs and provide guidance for the inactivation of enzymes and the processing of lily bulb juice.
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