54315-41-2Relevant academic research and scientific papers
ENENTIOSELECTIVE HYDROLYSES BY BAKER'S YEAST - III. MICROBIAL RESOLUTION OF ALKYNYL ESTERS USING LYOPHILIZED YEAST
Glaenzer, B. I.,Faber, K.,Griengl, H.
, p. 5791 - 5796 (1987)
Both enantiomers of optically active 1-alkyn-3-ols were obtained in high optical purity by microbial resolution of their racemic acetate using a stable ready-to-use lyophilized yeast preparation.
Ester Synthesis in Water: Mycobacterium smegmatis Acyl Transferase for Kinetic Resolutions
de Leeuw, Nicolas,Torrelo, Guzman,Bisterfeld, Carolin,Resch, Verena,Mestrom, Luuk,Straulino, Emanuele,van der Weel, Laura,Hanefeld, Ulf
, p. 242 - 249 (2017/11/16)
The acyl transferase from Mycobacterium smegmatis (MsAcT) catalyses transesterification reactions in aqueous media because of its hydrophobic active site. Aliphatic cyanohydrin and alkyne esters can be synthesised in water with excellent and strikingly opposite enantioselectivity [(R);E>37 and (S);E>100, respectively]. When using this enzyme, the undesired hydrolysis of the acyl donor is an important factor to take into account. Finally, the choice of acyl donor can significantly influence the obtained enantiomeric excesses. (Figure presented.).
Novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents
Abad, Jose-Luis,Soldevila, Carles,Camps, Francisco,Clapes, Pere
, p. 5351 - 5356 (2007/10/03)
A novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents is described. The key step is the kinetic lipase-catalyzed resolution of racemic mixtures of substituted propargylic alcohols. The efficiency of this new approach was tested in the preparation of the corresponding enantiomers of 1,11-hexadecandiol derivatives ((R)-5 and (S)-5). Two strategies were tested. In the first one, the racemic intermediate 1-octyn-3-ol (1) was resolved enzymatically and then elongated with 1-bromo-9,11-dioxadodecane. Alternatively, the racemic 1 can be elongated to the corresponding racemic 17,19-dioxa-7-eicosyn-6-ol (3) first and then resolved biocatalytically. Twelve commercially available lipases were screened for the kinetic resolution of these intermediates. Among them, Candida antarctica lipase (CAL-B) and Humicola lanuginosa lipase (HLL) were the best biocatalysts for the resolution of 1 (S enantiomer 90% ee, E = 35), and 3 (R enantiomer 90% ee, E = 34), respectively.
Enzymic Resolution of (+/-)-Acyclic Alcohols via Asymmetric Hydrolysis of Corresponding Acetates by Microorganisms
Oritani, Takayuki,Yamashita, Kyohei
, p. 2407 - 2412 (2007/10/02)
Asymmetric hydrolysis of (+/-)-1-pentyl-2-propynyl and 1-pentyl-2-propenyl acetates by selected microorganisms produced chiral 1-octyn-3-ol and 1-octen-3-ol, respectively, with high optical purities and acetates of their antipodes.Enantioselectivity of microbial hydrolysis changed with the microorganisms used.Also, (+/-)-1-ethylhexyl acetate was asymmetrically hydrolyzed by microorganisms to give (S)-3-octanol and (R)-1-ethylhexyl acetate of relatively low optical purity and hydrolytic ratio, compared with those of (+/-)-1-pentyl-2-propynyl acetate.
