Purification and Some Properties of Carboxylesterase from<i>Arthrobacter globiformis</i>; Stereoselective Hydrolysis of Ethyl Chrysanthemate

Nishizawa, Masako; Gomi, Hideyuki; Kishimoto, Fumitaka

doi:10.1271/bbb.57.594

Cited by 35 publications

(27 citation statements)

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“…1) All the kinetical values were measured using (+)-trans ethyl chrysanthemate as substrate at 45 C unless otherwise mentioned, and the resulting (+)-trans chrysanthemic acid was analyzed by gas chromatography as described previously. 2) Kinetic values such as Vmax and Km were measured by LineweaverBurk plot. In some cases, (+)-trans p-nitrophenyl chrysanthemate or phenolphthalein dibutyrate was also used, and the enzymatic activity was determined by measuring the amount of liberated p-nitrophenol or phenolphthalein with a spectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

“…Masako NISHIZAWA, 1;y Yoshiyasu YABUSAKI, 2 and Masaharu KANAOKA Carboxylesterase of Arthrobacter globiformis is a unique enzyme that stereoselectively hydrolyzes ethyl chrysanthemate. In a previous study, 1) we performed cloning and overexpression of the esterase gene.…”

Section: Identification Of the Catalytic Residues Of Carboxylesterasementioning

confidence: 99%

“…We used DFP, a common serine hydrolase inhibitor that inhibits the enzymatic activity of the esterase of A. globiformis as well, 2) as an active-site probe in subsequent analysis.…”

Section: Dfp Labeling and Mass Spectrometric Analysis Of The Esterasementioning

confidence: 99%

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Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

Nishizawa¹,

Yabusaki

Kanaoka³

2011

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Section: Identification Of the Catalytic Residues Of Carboxylesterasementioning

confidence: 99%

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Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

Nishizawa¹,

Yabusaki

Kanaoka³

2011

Bioscience, Biotechnology, and Biochemistry

Self Cite

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“…Some esterases may be involved in plant pathogenicity, carbon source provision and biocide detoxification [67], others catalyze inter-esterification, aminolysis, and peracid formation [68]. Not only this; lipases and esterases have also been used successfully in organic synthesis of optically pure substances, perfumes and antioxidants [7,[69][70][71][72][73][74][75][76].…”

Section: Correlation Between Biosurfactant Production and Esterase Acmentioning

confidence: 99%

Biosurfactant Production and Potential Correlation with Esterase Activity

Sekhon¹

2012

J Pet Environ Biotechnol

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Biosurfactants (microbial surfactants) are surface active compounds produced extracellularly or as part of the cell membrane by several bacterial and fungal species. They have the unique property of reducing the surface and interfacial tension of liquids. Biosurfactants have applications in the field of agriculture, petroleum, microbial enhanced oil recovery, biomedical sciences, cosmetics, food processing and pharmaceuticals. The global biosurfactants market has grown gradually. Regardless of their greater biodegradability and reduced toxicity, cost competitiveness still remains the major concern for biosurfactant production. However, recombinant or metabolically engineered hyper producing strains combined with optimized cultivation conditions have made it possible for many companies to reap the benefits of 'green' biosurfactant technology. Simultaneously, biosurfactants and bioemulsifiers showing esterase activities and having potential applications are reported to form stable oil-water emulsions with hydrophobic substrates such as hexadecane and polyaromatic hydrocarbons. Biosurfactant production and release of esterases by the microbial cells is shown to be synchronized and symbiotically beneficial in some species. Several bacterial biosurfactant and esterase genes have been identified, cloned and expressed for their enhanced production. This

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“…They include the enzymes from Bacillus stearothermophilus,11.12) Bacillus subtilis, 13,14) Aspergillus niger,15) Aspergillus awamori, 16) Pseudomonas cepacia,17) Pseudomonas fluorescens, 18,19) Ochrobactrum anthropi, 20) baker's yeast, 21) and Arthrobactrum globiformis. 22 ) We previously reported purification and characterization of a thermostable lipase from Pseudomonas sp. 23) and cloning of the lipase gene.…”

mentioning

confidence: 99%

Purification and Characterization of a Carboxylesterase fromPseudomonassp. KWI-56

Sugihara

Shimada

Nagao

et al. 1994

Bioscience, Biotechnology, and Biochemistry

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Purification and Some Properties of Carboxylesterase fromArthrobacter globiformis; Stereoselective Hydrolysis of Ethyl Chrysanthemate

Cited by 35 publications

References 1 publication

Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

Biosurfactant Production and Potential Correlation with Esterase Activity

Purification and Characterization of a Carboxylesterase fromPseudomonassp. KWI-56

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