Purification and comparison of soluble and membrane-bound polyphenol oxidase from potato (Solanum tuberosum) tubers

文献类型： 外文期刊

第一作者： Liu, Hui

作者： Liu, Hui;Hu, Deyu;Wang, Hui;Liu, Hui;Pan, Mu;Lu, Yang;Wang, Mei;Huang, Shan;Li, Jun;Luo, Ke;Luo, Linli;Yao, Mingyong;Wang, Hui

作者机构：

关键词： Enzymatic browning; Potato; sPPO; mPPO; Enzyme properties

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.6； 五年影响因子：1.6 ）

ISSN： 1046-5928

年卷期： 2023 年 202 卷

页码：

收录情况： SCI

摘要： Enzymatic browning greatly affects the quality of potato products. Polyphenol oxidase (PPO) is the enzyme mainly responsible for potato enzymatic browning. PPO has soluble polyphenol oxidase (sPPO) and membrane -bound polyphenol oxidase (mPPO) forms. In this study, the properties of sPPO and mPPO were investigated in potato tubers. The molecular weight of potato sPPO and mPPO were estimated to be 69 kDa in the form of homodimers in vivo. The mass spectrometry results showed that the purified sPPO and mPPO protein in potato tubers was mainly tr|M1BMR6 (Uniprot). The optimum pH for sPPO and mPPO was 6.5, and the optimum temperatures were 20 and 30 degrees C, respectively. The Michaelis constant (Km) and maximum unit enzyme activity (Vmax) of sPPO were 6.08 mM and 2161 U/S when catechol was used as the substrate, whereas those of mPPO were 2.95 mM and 2129.53 U/S, respectively. The mPPO had stronger affinity to the substrate catechol than sPPO, whereas pyrogallic acid was stronger affinity for sPPO. Ascorbic acid and sodium sulfite were inhibitors of sPPO and mPPO, respectively. After understanding the different binding states of polyphenol oxidase, different inhibitors and treatment methods can be used to treat the enzyme according to different enzymatic properties, so as to achieve a greater degree of Browning control. These results will provide a theoretical basis for regulating PPO activity to reduce enzymatic browning during potato processing.

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