Characterisation of aldo-keto reductases from Lactobacillus reuteri DSM20016. (November 2022)

• Record Type: Journal Article
• Authors: Qu, Wenhao; Bai, Yajun; Fan, Tai-Ping; Zheng, Xiaohui; Cai, Yujie
• Is Part Of: Process biochemistry. Volume 122(2022)Supplement Part 2
• Page Start: 172
• Page End: 180
• Publication Date: 2022-11
• Subjects: Lactobacillus reuteri -- Aldo-keto reductases -- Flavored aldehyde -- 3-hydroxypropionaldehyde; 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.2022.10.001
• Languages: English
• ISSNs: 1359-5113

Abstract

Abstract: Lactobacillus reuteri DSM20016 has several aldo-keto reductases (AKRs), and they were heterologously expressed in E. coli BL21 (DE3) in this study. Subsequently, these AKRs were purified, and their enzymatic properties were investigated. It was found that these enzymes used NADPH as coenzyme and did not depend on metal ions. The optimum pH of these AKRs was a slightly acidic (AKR-1 and AKR-6: 5.5; AKR-3 and AKR-8: 6; AKR-2 and AKR-4: 6.5). These enzymes had a broad substrate spectrum and could convert a variety of aldehydes to alcohols; however, they did not catalyze the reverse reactions. All results showed that Lactobacillus reuteri had the ability to produce various volatile compounds, which allowed Lactobacillus reuteri to impart complex aroma to something. Graphical Abstract: ga1 Highlights: Comprehensive excavation of aldo-keto reductases in Lactobacillus reuteri. These aldo-keto reductases have a broad spectrum of substrates and can reduce various aldehydes. Characterization of the enzymatic properties of aldo-keto reductases from Lactobacillus reuteri.