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3-Hydroxypropionaldehyde-specific aldehyde dehydrogenase from Bacillus subtilis catalyzes 3-hydroxypropionic acid production in Klebsiella pneumoniae  ( EI收录)  

文献类型:期刊文献

英文题名:3-Hydroxypropionaldehyde-specific aldehyde dehydrogenase from Bacillus subtilis catalyzes 3-hydroxypropionic acid production in Klebsiella pneumoniae

作者:Su, Mingyue[1]; Li, Ying[1]; Ge, Xizhen[2]; Tian, Pingfang[1]

第一作者:Su, Mingyue

通讯作者:Tian, Pingfang

机构:[1] Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China; [2] College of Biochemical Engineering, Beijing Union University, Beijing, 100023, China

第一机构:Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China

年份:2015

卷号:37

期号:3

起止页码:717-724

外文期刊名:Biotechnology Letters

收录:EI(收录号:20144900286831);Scopus(收录号:2-s2.0-84925489920)

语种:英文

外文关键词:Bacteria - Bacteriology - Catalyst activity - Aldehydes - Substrates

摘要:In Klebsiella pneumoniae, aldehyde dehydrogenases (ALDH) convert 3-hydroxypropionaldehyde (3-HPA) into 3-hydroxypropionic acid (3-HP). Although ALDHs can increase the production of 3-HP in K. pneumoniae, the substrate specificity of ALDH homologues from other microorganisms toward 3-HPA is less documented. Here we report that DhaS, a putative ALDH from Bacillus subtilis, shows high specificity toward 3-HPA when heterologously expressed in K. pneumoniae. Using NAD+ as a cofactor, DhaS exhibited higher catalytic activity (2.3 U mg?1) and lower Km value (0.4?mmol?l?1) toward 3-HPA than that toward other aldehydes. Under shake-flask conditions, the recombinant strain produced 2.1?g 3-HP l?1 in 24?h, which is 3.9-fold of that in a control harboring a blank vector. Under non-optimized bioreactor conditions, the recombinant strain produced 18?g 3-HP l?1 and 1,3-propanediol (1,3-PDO) at 27?g?l?1 in 24?h. The overall conversion rate from glycerol to 3-HP and 1,3-PDO reached 59.4?mol?mol?1. Homology modeling of DhaS illustrates substrate specificity and NAD+-binding site. DhaS is thus a 3-HPA-specific enzyme useful for production of 3-HP. ? 2014, Springer Science+Business Media Dordrecht.

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