Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)-ketoprofen ethyl ester

Choi, Gi-Sub; Kim, Ji-Youn; Kim, Ji-Heui; Ryu, Yeon‐Woo; Kim, Geun-Joong

doi:10.1016/s1046-5928(03)00009-3

Cited by 33 publications

(14 citation statements)

References 24 publications

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“…Esterases (EC 3.1.1.1) hydrolyze the ester bonds of water-soluble fatty acid esters with shortchain acyl groups (6C8) (Verger 1997;Ollis et al 1992). Several methods have been developed to screen and isolate novel esterases (Kumar et al 2012;Elend et al 2006;Kim et al 2006;Choi et al 2003;Suzuki et al 2003), including metagenomic techniques (Henne et al 2000). A range of esterase characteristics have been described, primarily in molecular biology, targeted synthesis, purification, quantitation, production, and distribution.…”

Section: Esterasesmentioning

confidence: 99%

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017

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Abstract:In the pulp and paper industry, during the manufacturing process, the agglomeration of pitch particles (composed of triglycerides, fatty acids, and esters) leads to the formation of black pitch deposits in the pulp and on machinery, which impacts on the process and pulp quality. Traditional methods of pitch prevention and treatment are no longer feasible due to environmental impact and cost. Consequently, there is a need for more efficient and environmentally friendly approaches. The application of lipolytic enzymes, such as lipases and esterases, could be the sustainable solution to this problem. Therefore, an understanding of their structure, mechanism, and sources are essential. In this report, we review the microbial sources for the different groups of lipolytic enzymes, the differences between lipases and esterases, and their potential applications in the pulping industry.

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Section: Esterasesmentioning

confidence: 99%

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017

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“…In general, 50-100 colonies were visible after proper dilution. The positive clones were selected by activity staining using Fast Blue B (15 mg/ml) and ␣-naphthyl acetate (45 mg/ml) and insert DNA was purified using a large plasmid preparation method [14]. Then, DNA was partially digested with NotI, KpnI, ClaI and HindIII to collect 1-10 kb DNA fragments.…”

Section: Library Screening and Sequence Analysismentioning

confidence: 99%

“…The protein concentration was determined using BioRad Protein Assay kit (Dye Reagent Concetnrate), with bovine serum albumin (BSA) as a standard (R 2 = 0.9974). SDS-PAGE and activity staining with native-PAGE were done as previously described [14,16,17]. …”

Section: Expression and Purification Of Recombinant Esterasementioning

confidence: 99%

Identification and characterization of a novel (S)-ketoprofen-specific esterase

Yoon

Kim

Ryu

et al. 2007

International Journal of Biological Macromolecules

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“…In order to synthesize chiral reagents by chemo-enzymatic methods, recombinant techniques have been employed in order to express and purify useful microbial enzymes. 14) These recombinant proteins have been purified on an affinity resin, Ni-NTA, in a single step, through the addition of a hexa-histidine tag to the N-terminus. Furthermore, recent genetic approaches have progressed dramatically.…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

Site-Specific and Asymmetric Hydrolysis of Prochiral 2-Phenyl-1,3-propanediol Diacetate by a Bacterial Esterase from an Isolated Strain

Mitsui

Shinya

Ichiyama

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Bacillus cereus 809A and Burkholderia sp. 711C were isolated from soil. These strains demonstrate hydrolysis activity towards prochiral 2-phenyl-1,3-propanediol diacetate and accumulated the corresponding chiral monoacetates into the reaction mixture. When 2-phenyl 1,3-propanediol diacetate was used as a substrate, the produced monoacetates with Burkholderia sp. 711C were obtained in a racemic form but that produced by Bacillus cereus 809A showed an excess of the (S)-form. The resting cell reaction revealed that for Bacillus cereus 809A, there was an enrichment of one of the enantiomers of the monoacetate such that the enantiomeric excess (e.e.) of the (S)-form was over 95%. The purified enzyme from Bacillus cereus 809A hydrolyzed diacetate to monoacetate, and the e.e. value of the (S)-form increased by prolonged reaction in a way similar to the resting cell reaction. From N-terminal amino acids, this esterase is conserved in some strains of Bacillus for which the genomic sequences have been reported.

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Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)-ketoprofen ethyl ester

Cited by 33 publications

References 24 publications

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

Identification and characterization of a novel (S)-ketoprofen-specific esterase

Site-Specific and Asymmetric Hydrolysis of Prochiral 2-Phenyl-1,3-propanediol Diacetate by a Bacterial Esterase from an Isolated Strain

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