73104-88-8Relevant articles and documents
Resolution of (R,S)-1-(4-methoxyphenyl)ethanol by lipase-catalyzed stereoselective transesterification and the process optimization
He, Bingbing,Tang, Fengci,Sun, Chenrui,Su, Jiahao,Wu, Bingcheng,Chen, Yan,Xiao, Yuquan,Zhang, Panliang,Tang, Kewen
, p. 438 - 445 (2021/12/17)
An efficient lipase-catalyzed stereoselective transesterification reaction system was established for resolution of 1-(4-methoxyphenyl)ethanol (MOPE) enantiomers. A series of lipases were tested and compared. The immobilized lipase Novozym 40086 is selected as the best choice. The effects of organic solvent, acyl donor, time and temperature on substrate conversion (c), and optical purity of the remaining substrate (eeS) were investigated. Response surface methodology and central composite design were employed to evaluate the effect of some important factors and to optimize the process. Under the optimized conditions including solvent of n-hexane, acyl donor of vinyl acetate, temperature of 35°C, substrate molar ratio of 1:6, enzyme dosage of 20 mg, and reaction time of 2.5 h, eeS of 99.87% with c of 56.71% is achieved. The use of alkane solvent and immobilized enzyme, the mild reaction conditions, and the reduced reaction time make the system promising in industrial application.
Activity and specificity studies of the new thermostable esterase EstDZ2
Myrtollari, Kamela,Katsoulakis, Nikolaos,Zarafeta, Dimitra,Pavlidis, Ioannis V.,Skretas, Georgios,Smonou, Ioulia
, (2020/09/16)
In this paper, we study the activity and specificity of EstDZ2, a new thermostable carboxyl esterase of unknown function, which was isolated from a metagenome library from a Russian hot spring. The biocatalytic reaction employing EstDZ2 proved to be an efficient method for the hydrolysis of aryl p-, o- or m-substituted esters of butyric acid and esters of secondary alcohols. Docking studies revealed structural features of the enzyme that led to activity differences among the different substrates.
LipG9-mediated enzymatic kinetic resolution of racemates: Expanding the substrate-scope for a metagenomic lipase
Thomas, Juliana Christina,Alnoch, Robson Carlos,Costa, Allen Carolina dos Santos,Bandeira, Pamela Taisline,Burich, Martha Daniela,Campos, Suelem Kluconski,de Oliveira, Alfredo Ricardo Marques,de Souza, Emanuel Maltempi,Pedrosa, Fabio de Oliveira,Krieger, Nadia,Piovan, Leandro
, (2019/05/22)
Enzymes are the main biocatalysts of biological systems and nowadays they play an important role in asymmetric organic synthesis. Microorganisms are the main source for enzymes, however, just a very small portion of them are culturable at lab conditions and, as an alternative, metagenomics approaches allow new enzymes to be accessed from so-called “non-culturable” microorganisms. Several classes of metagenomic enzymes have been described in literature. Nevertheless, studies about their potential for asymmetric biotransformation are underexploited. Therefore, we present our recent efforts to establish the substrate-scope of LipG9, a metagenomic lipase, in enzymatic kinetic resolution (EKR) of chiral substances. LipG9 was previously isolated, immobilized and successfully applied in EKR of aliphatic alcohols. In this study, a series of resolvable chiral substances were assayed with LipG9, and secondary benzyl alcohols/esters were preferentially resolved in a much superior enantioselectivity (E > 200) than those described for aliphatic alcohols (E from 4 to 63). In an opposite way, Im-LipG9 did not present activity for tertiary alcohols, amines and lactones. When compared to commercial lipases, Im-LipG9 enantioselectivity was superior to Candida rugosa lipase and equivalent to Candida antarctica lipase B. Thus, the chemo and enantioselectivity of LipG9 in EKR reactions were identified and its potential for asymmetric synthetic approaches was demonstrated.
