78183-56-9Relevant articles and documents
Efficient (3S)-acetoin and (2S, 3S)-2, 3-butanediol production from meso-2, 3-butanediol using whole-cell biocatalysis
He, Yuanzhi,Chen, Feixue,Sun, Meijing,Gao, Huifang,Guo, Zewang,Lin, Hui,Chen, Jiebo,Jin, Wensong,Yang, Yunlong,Zhang, Liaoyuan,Yuan, Jun
, (2018/03/27)
(3S)-Acetoin and (2S, 3S)-2, 3-butanediol are important platform chemicals widely applied in the asymmetric synthesis of valuable chiral chemicals. However, their production by fermentative methods is difficult to perform. This study aimed to develop a whole-cell biocatalysis strategy for the production of (3S)-acetoin and (2S, 3S)-2, 3-butanediol from meso-2, 3-butanediol. First, E. coli co-expressing (2R, 3R)-2, 3-butanediol dehydrogenase, NADH oxidase and Vitreoscilla hemoglobin was developed for (3S)-acetoin production from meso-2, 3-butanediol. Maximum (3S)-acetoin concentration of 72.38 g/L with the stereoisomeric purity of 94.65% was achieved at 24 h under optimal conditions. Subsequently, we developed another biocatalyst co-expressing (2S, 3S)-2, 3-butanediol dehydrogenase and formate dehydrogenase for (2S, 3S)-2, 3-butanediol production from (3S)-acetoin. Synchronous catalysis together with two biocatalysts afforded 38.41 g/L of (2S, 3S)-butanediol with stereoisomeric purity of 98.03% from 40 g/L meso-2, 3-butanediol. These results exhibited the potential for (3S)-acetoin and (2S, 3S)-butanediol production from meso-2, 3-butanediol as a substrate via whole-cell biocatalysis.
Enantioselective hydrogenation of activated ketones in the presence of Pt-cinchona catalysts. Is the proton transfer concept valid?
Margitfalvi, József L.,Tálas, Emília
, p. 142 - 145 (2014/01/17)
Experimental evidences related to the proton transfer in the catalytic system Pt-cinchona alkaloids for enantioselective hydrogenation of activated ketones were collected and analyzed. Both new and earlier results indicate that in aprotic media direct transfer of proton from platinum to the substrate with the involvement of quinuclidine nitrogen as a general rule can be questioned.
Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: From C-C bond cleavage to C-C bond ligation
Loschonsky, Sabrina,Wacker, Tobias,Waltzer, Simon,Giovannini, Pier Paolo,McLeish, Michael J.,Andrade, Susana L. A.,Müller, Michael
supporting information, p. 14402 - 14406 (2015/02/19)
ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzes the CC bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate. One of the two reactivities of CDH was selectively knocked down by mutation experiments. CDH-H28A is much less able to catalyze the CC bond formation, while the ability for CC bond cleavage is still intact. The double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94% enantiomeric excess. In addition to pyruvate, methyl pyruvate and butane-2,3-dione are alternative donor substrates for CC bond formation. Thus, the very rare aldehyde-ketone cross-benzoin reaction has been solved by design of an enzyme variant.