Production of 2-butanol through meso-2, 3-butanediol consumption in lactic acid bacteria

• Published in: FEMS microbiology letters Vol. 360; no. 1; pp. 70 - 75
• Main Authors: Ghiaci, Payam, Lameiras, Francisca, Norbeck, Joakim, Larsson, Christer
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.11.2014; Oxford University Press
• Subjects: Bacteria; biofuel; Biofuels; Butanols - analysis; Butanols - metabolism; Butylene Glycols - metabolism; Industrial Microbiology; lactic acid bacteria; Lactobacillus brevis - isolation & purification; Lactobacillus brevis - metabolism; microbial biochemistry; Microbiology; microbial biochemistry; biofuel; lactic acid bacteria
• ISSN: 0378-1097; 1574-6968; 1574-6968
• DOI: 10.1111/1574-6968.12590

Abstract 2-Butanol has been an issue of industries in many areas, for example, biofuel production (as an advanced alternate fuel), fermented beverages, and food (as taste-altering component). Thus, its source of production, the biological pathway, and the enzymes involved are of high interest. In this study, 42 different isolates of lactic acid bacteria from nine different species were screened for their capability to consume meso-2, 3-butanediol and produce 2-butanol. Lactobacillus brevis was the only species that showed any production of 2-butanol. Five of ten tested isolates of L. brevis were able to convert meso-2, 3-butanediol to 2-butanol in a synthetic medium (SM2). However, none of them showed the same capability in a complex medium such as MRS indicating that the ability to produce 2-butanol is subject to some kind of repression mechanism. Furthermore, by evaluating the performance of the enzymes required to convert meso-2, 3-butanediol to 2-butanol, that is, the secondary alcohol dehydrogenase and the diol dehydratase, it was shown that the latter needed the presence of a substrate to be expressed. Lactobacillus brevis possesses a diol dehydratase, the expression of which is substrate- and medium-dependent. Lactobacillus brevis possesses a diol dehydratase, the expression of which is substrate- and medium-dependent.