A green, fully enzymatic procedure for amine resolution, using a lipase and a penicillin G acylase

Ismail, Hilda; Lau, Rute Madeira; Langen, Luuk M. van; Rantwijk, Fred van; Švedas, Vytas K.; Sheldon, Roger A.

doi:10.1039/b714088f

Cited by 29 publications

(16 citation statements)

References 19 publications

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“…Alternatively, when penicillin amidase was used to catalyze the amide hydrolysis step, a much faster reaction was observed. 212 More recently, the generality of the lipase-catalyzed aminolysis of carboxylic acid esters was further established with the demonstration that Pseudomonas stutzeri lipase catalyzes ester aminolysis with a broad range of esters and amines, including bulky esters and secondary amines. 213 Another pertinent example of an enzymatic reaction involving non-natural nucleophiles is the ring opening of epoxides catalyzed by halohydrin dehalogenases (HHDHs).…”

Section: Chemical Reviewsmentioning

confidence: 99%

Role of Biocatalysis in Sustainable Chemistry

2017

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Based on the principles and metrics of green chemistry and sustainable development, biocatalysis is both a green and sustainable technology. This is largely a result of the spectacular advances in molecular biology and biotechnology achieved in the past two decades. Protein engineering has enabled the optimization of existing enzymes and the invention of entirely new biocatalytic reactions that were previously unknown in Nature. It is now eminently feasible to develop enzymatic transformations to fit predefined parameters, resulting in processes that are truly sustainable by design. This approach has successfully been applied, for example, in the industrial synthesis of active pharmaceutical ingredients. In addition to the use of protein engineering, other aspects of biocatalysis engineering, such as substrate, medium, and reactor engineering, can be utilized to improve the efficiency and cost-effectiveness and, hence, the sustainability of biocatalytic reactions. Furthermore, immobilization of an enzyme can improve its stability and enable its reuse multiple times, resulting in better performance and commercial viability. Consequently, biocatalysis is being widely applied in the production of pharmaceuticals and some commodity chemicals. Moreover, its broader application will be further stimulated in the future by the emerging biobased economy.

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Section: Chemical Reviewsmentioning

confidence: 99%

Role of Biocatalysis in Sustainable Chemistry

2017

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“…It is well reported in the literature that toluene and ether are usually the best solvent options for the acylation of amines catalyzed by CALB to obtain high yield and selectivity. 19,20,21,22 A variety of organic solvents with different polarity were screened. When using THF as the solvent, the best result of enantioselectivity factor E = 31 (87% ee value and 45% conversion) for acylation of 1a was achieved (Table 2).…”

Section: Kinetic Resolutionmentioning

confidence: 99%

Chemoenzymatic dynamic kinetic resolution of α-trifluoromethylated amines: influence of substitutions on the reversed stereoselectivity

Cheng

Xia

et al. 2013

RSC Adv.

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Enzymatic resolution of a-trifluoromethylated amines via kinetic resolution (KR), dynamic kinetic resolution (DKR) employing CALB-Pd/Al 2 O 3 , and a one-pot sequential process of KR/DKR/KR was investigated comparatively for the first time. Although CALB-catalyzed KR of a-trifluoromethylated amines with substituents of methyl (1a), isopropyl (1c), phenyl (1d) and benzyl group (1e) can provide good stereoselectivity factors E from 31 to .200 respectively, DKR and sequential process of KR/DKR/KR possess better practical application potential because of the higher conversion (62%-84%) and the similar enantiomeric excesses (90%-99%). The enantiopreference and inversion for the a-trifluoromethylated amines displayed by CALB were observed and explained by docking modes. Namely, for 1,1,1-trifluoro-2propylamine (1a), the product amide with R-configuration was obtained, and the enantiopreference was converted to S for the amines (1b-1e) with substituents larger than methyl group. The catalysts recycle, and scale-up experiments were demonstrated successfully. All these results indicated the high efficiency and green feature of this enzymatic process, and its application significance.

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“…Hence, it can hydrolyze different compounds attached to the phenylacetyl group through an amide bond. It has also been shown to act on substrates with an N-acetyl group (Cole, 1969).This broad spectrum activity of PGA has been exploited in the resolution of racemic mixtures (Cardillo et al, 1996;Ismail et al, 2008;van Langen et al, 2000), as the enzyme specifically cleaves the amide bond of only the L-isomer of the phenylacylated derivative (van Langen et al, 2000). Mutant forms of cephalosporin acylase have also been reported to accept amino acids in place of the b-lactam group (Sio et al, 2002).…”

Section: Catalytic Mechanism and Structural Organizationmentioning

confidence: 97%

Penicillin acylases revisited: importance beyond their industrial utility

Avinash

Pundle

Ramasamy

et al. 2014

Critical Reviews in Biotechnology

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It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus paving the way for production of newer semi-synthetic antibiotics. They are classified according to the type of penicillin (G or V) that they preferentially hydrolyze. Penicillin acylases are also used in the resolution of racemic mixtures and peptide synthesis. However, it is rather unfortunate that the focus on the use of penicillin acylases for industrial applications has stolen the spotlight from the study of the importance of these enzymes in natural metabolism. The penicillin acylases, so far characterized from different organisms, show differences in their structural nature and substrate spectrum. These enzymes are also closely related to the bacterial signalling phenomenon, quorum sensing, as detailed in this review. This review details studies on biochemical and structural characteristics of recently discovered penicillin acylases. We also attempt to organize the available insights into the possible in vivo role of penicillin acylases and related enzymes and emphasize the need to refocus research efforts in this direction.

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A green, fully enzymatic procedure for amine resolution, using a lipase and a penicillin G acylase

Cited by 29 publications

References 19 publications

Role of Biocatalysis in Sustainable Chemistry

Role of Biocatalysis in Sustainable Chemistry

Chemoenzymatic dynamic kinetic resolution of α-trifluoromethylated amines: influence of substitutions on the reversed stereoselectivity

Penicillin acylases revisited: importance beyond their industrial utility

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