文献类型： 外文期刊

第一作者： Qin Gaihua

作者： Qin Gaihua;Liu Chunyan;Gao Zhenghui;Li Jiyu;Qi Yongjie;Pan Haifa;Yi Xingkai;Xu Yiliu;Qin Gaihua;Liu Chunyan;Gao Zhenghui;Li Jiyu;Qi Yongjie;Xu Yiliu

作者机构：

关键词： recombinant protein; oxidase; fruit aroma; enzyme activity

期刊名称：EUROPEAN JOURNAL OF HORTICULTURAL SCIENCE （ 影响因子：1.074； 五年影响因子：1.641 ）

ISSN： 1611-4426

年卷期： 2022 年 87 卷 1 期

页码：

收录情况： SCI

摘要： Alcohol dehydrogenase (ADH) is an oxidation-reduction enzyme that catalyzes interconversion of alcohols and aldehydes and provides a substrate for the formation of esters. Although candidate genes encoding ADHs have been identified in pear fruits, the characterization of their encoded proteins remains unknown. In this study, an ADH was cloned from a cDNA of Pyrus ussuriensis 'Nanguoli' (PuADH2) and was expressed in Escherichia coli. The recombinant PuADH2 protein was purified and subject to biochemical characterization. PuADH2 was more likely an oxidative enzyme independent of substrate specificity. During oxidation reaction, no preference for coenzyme factors (NAD(+) and NADP(+)) for PuADH2 oxidase activity. In addition, the oxidation activity of PuADH2 slightly increased with high K+ concentrations, but significantly decreased with Zn2+. These results provide insights into PuADH2 as an oxidase and promote future study on the synthesis and regulation of aromatic compounds in pear fruits.

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