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, PF[1]

机构：[1]Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China;[2]Beijing Union Univ, Coll Biochem Engn, Beijing 100023, Peoples R China

第一机构：Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China

通讯机构：[1]corresponding author), Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R 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：;WOS:【SCI-EXPANDED(收录号:WOS:000350394800031)】；

基金：This work was supported by Grants from National Basic Research Program of China (973 Program) (2012CB725200) and National Natural Science Foundation of China (No. 21076013, 21276014).

语种：英文

外文关键词：Aldehyde dehydrogenase; Glycerol; 3-Hydroxypropionaldehyde; 3-Hydroxypropionic acid; Klebsiella pneumoniae; Substrate specificity

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 K (m) 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.