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작성일 : 16-09-21 10:44

(2016, IF=2.529) Molecular cloning and expression of Enterobacter aerogenes α-acetolactate decarboxylase in pyruvate decarboxylase-deficient Saccharomyces cerevisiae for efficient 2,3-butanediol production

글쓴이 : ycpark

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http://dx.doi.org/10.1016/j.procbio.2015.11.023 [1064]

Molecular cloning and expression of Enterobacter aerogenes α-acetolactate decarboxylase in pyruvate decarboxylase-deficient Saccharomyces cerevisiae for efficient 2,3-butanediol production

Myeong-Hyeon Choi, Soo-Jung Kim, Jin-Woo Kim, Yong-Cheol Park, Jin-Ho Seo

Process Biochemistry, 51(2): 170-176, 2016.(2016.02)

α-Acetolactate decarboxylase (ALDC) catalyzes the conversion of α-acetolactate into acetoin, a precursor of 2,3-butanediol (2,3-BD). In this study, we overexpressed the genes coding for various ALDCs from natural 2,3-BD producing bacteria in recombinant Saccharomyces cerevisiae SB strains with two essential enzymes for 2,3-BD production (α-acetolactate synthase and 2,3-BD dehydrogenase) and without pyruvate decarboxylase (PDC) activity. Expression of ALDCs from Bacillus subtilis and Enterobacter aerogenes gave 1.3–1.5 times higher 2,3-BD productivities than those from Klebsiella pneumoniae and Klebsiella oxytoca oxytoca. Kinetic analysis of purified ALDCs revealed that E. aerogenes ALDC exhibited an 1.7 fold higher kcat/Km (22.9 ± 0.2 mM−1 s−1) than B. subtilis ALDC (13.3 ± 4.1 mM−1 s−1). In fed-batch fermentations by intermittent addition of a concentrated glucose solution, the SB-Ea strain overexpressing E. aerogenes ALDC produced 132.4 g/L of 2,3-BD with a yield of 0.34 g 2,3-BD/g glucose and 0.41 g/L h productivity, which were 30% and 25% higher than those of the BD4 strain expressing B. subtilis ALDC. It was concluded that E. aerogenes ALDC was the most effective enzyme among four bacterial ALDCs for improving 2,3-BD production in PDC-deficient S. cerevisiae.

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