Characterizing the effect of S-nitrosoglutathione on Saccharomyces cerevisiae: Upregulation of alcohol dehydrogenase and inactivation of aconitase. (February 2022)

• Record Type: Journal Article
• Authors: Sengupta, Swarnab; Nath, Rohan; Bhattacharjee, Arindam
• Is Part Of: Process biochemistry. Volume 113(2022)
• Page Start: 62
• Page End: 70
• Publication Date: 2022-02
• Subjects: S. cerevisiae Saccharomyces cerevisiae -- SOD super oxide dismutase -- HClO4 perchloric acid -- KOH potassium hydroxide -- DTNB 5, 50-dithio-bis (2-nitrobenzoic acid) -- PBS phosphate Buffer Solution -- TCA trichloroacetic acid -- CTAB hexadecyltrimethylammoniumbromide -- KMnO4 potassium permanganate -- DNS 3, 5-dinitrosalicylic acid -- qPCR Quantitative Real-time PCR -- cDNA complementary DNA -- SD standard deviation; Saccharomyces cerevisiae -- Aconitase -- Nitrosative stress -- GSNO -- adh3; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2021.12.011
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: Highlights: Under nitrosative stress with GSNO, our result showed 1.4fold increase in ethanol production by Saccharomyces cerevisiae . Gene expression of adh3 was increased by 4 fold in the presence of GSNO. Whereas higher RNS level was observed but ROS level remained unchanged under GSNO stress. Blockage of aconitase may have caused metabolic shift from respiration to fermentation under GSNO stress. This process is eco-friendly, cost-effective and has a significant industrial potential in case of ethanol fermentation. Abstract: When exposed to nitrosative stress, the redox status of Saccharomyces cerevisiae changes significantly in vivo . Under nitrosative stress, aconitase, which catalyzes the conversion of citrate to isocitrate in the tricarboxylic acid (TCA) cycle, is known to be vulnerable. In this study, aconitase was completely repressed in the presence of 0.25 mM S -nitrosoglutathione (GSNO) as the nitrosative stress agent. Furthermore, a ∼1.5 fold increase in ethanol production and a 3.5 fold increase in alcohol dehydrogenase (ADH) activity were observed in the presence of 0.25 mM GSNO when compared to the control (untreated). Furthermore, we supported our findings with a gene expression study of the adh3 gene, which showed a 4 fold increase in the presence of 0.25 mM GSNO. This is the first report of its kind to characterize ethanol production under GSNO stress. This study may prove to be industrially significant in ethanol production.