Feedback inhibition of the prephenate dehydratase from Saccharomyces cerevisiae and its mutation in huangjiu (Chinese rice wine) yeast. (November 2020)

• Record Type: Journal Article
• Authors: Liu, Shuangping; Yang, Qilin; Mao, Jieqi; Bai, Mei; Zhou, Jiandi; Han, Xiao; Mao, Jian
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 133(2020)
• Publication Date: 2020-11
• Subjects: Prephenate dehydratase -- 2-Phenylethanol -- Specific activity -- Saccharomyces cerevisiae; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2020.110040
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: 2-Phenylethanol, an aromatic compound often found in fermented foods, is among the most abundant aromatic compounds in huangjiu (Chinese rice wine). The 2-phenylethanol found in huangjiu is produced by Saccharomyces cerevisiae HJ01, which produces much more 2-phenylethanol than the type strain, S. cerevisiae W303. Feedback regulation of 2-phenylethanol biosynthesis in S. cerevisiae has been carefully studied, except for the behavior of prephenate dehydratase (PDT; EC 4.2.1.51). Mutation (I161K, L239P and Q250H) in PDT were found in S. cerevisiae HJ01, and a structure-based analysis suggested the presence of conserved l -Phe binding sites. The purified PDT from S. cerevisiae strains HJ01 and W303 were found to be inhibited by l -Phe. The specific activity of the PDT HJ01 was 1.27-fold greater than that of the PDT W303 . It also showed greater substrate affinity ( K m, 11.1–15.9 mM), catalytic efficiency ( kcat / Km, 58.9 to 51.7 L/(mmols)), and thermal stability, but was less susceptible to feedback inhibition ( K i, 3.97 to 3.35 mM). Thus, mutations in the PDT from S. cerevisiae HJ01 contribute to the higher 2-phenylethanol concentration found in huangjiu . Highlights: Prephenate dehydratase (PDT) in S. cerevisiae was feedback inhibited by l -Phe. PDT in S. cerevisiae HJ01 showed greater substrate affinity, catalytic efficiency. Mutation of I161K, L239P and Q250H resulted less sensitive inhibition of l -Phe.