Determination and Characterization of Thermostable Esterolytic Activity from a Novel Thermophilic Bacterium Anoxybacillus gonensis A4

Faiz, Özlem; Çolak, Ahmėt; Saglam, Nagihan; Çanakçı, Sabriye; Beldüz, Ali Osman

doi:10.5483/bmbrep.2007.40.4.588

Cited by 32 publications

(18 citation statements)

References 30 publications

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“…Esterase activity was determined separately by using a spectrophotometric assay with p-nitrophenyl acetate (pNPA), p-nitrophenyl butyrate (pNPB), p-nitrophenyl laurate (pNPL) and p-nitrophenyl palmitate (pNPP) as substrates [22,23]. The reaction mixture was prepared by adding 1 mL of stock substrate solution (10 mM) to a final composition of 4:95 (v/v) of ethanol/buffer (50 mM Tris-HCl, pH 8.0), respectively.…”

Section: Determination Of Enzymatic Activity With Some P-nitrophenyl mentioning

confidence: 99%

A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: An extremely thermo- and pH-stable esterase

Yildirim

Çolak

Col

et al. 2009

Process Biochemistry

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Section: Determination Of Enzymatic Activity With Some P-nitrophenyl mentioning

confidence: 99%

A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: An extremely thermo- and pH-stable esterase

Yildirim

Çolak

Col

et al. 2009

Process Biochemistry

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“…In spite of the many uses of carboxylesterases, including the synthesis of esters and modification of triacylglycerols in the food industry, the resolution of racemic mixtures in the fine chemical and pharmaceutical industries, and the biodegradation of industrial waste and pesticides (Faiz et al . ; Lv et al . ), the industrial application of these enzymes is still limited (Bornscheuer ).…”

Section: Introductionmentioning

confidence: 99%

Carboxyl ester hydrolase from Penicillium expansum : cloning, characterization and overproduction by Penicillium griseoroseum

et al. 2013

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Aims: In this study, a gene that encodes a carboxylesterase (carb) in Penicillium expansum GF was cloned, sequenced and overexpressed by Penicillium griseoroseum PG63, and the enzyme was characterized. Methods and Results: The recombinant strain, P. griseoroseum T55, obtained upon transformation using the plasmid pAN-52-1-carb, showed integration of the carb gene into at least two heterologous sites of the genome by Southern blotting. Furthermore, the recombinant strain T55 exhibited almost a fourfold increase in carboxylesterase activity compared with PG63 strain when both were cultured without inducers. Based on the secondary structure and multiple sequence alignments with carboxylesterases, cholinesterase and lipase, a threedimensional model was obtained. The a/b barrel topology, that is typical of esterases and lipases, was indicated for the CARB protein with Ser 213 -Glu 341 -His 456 as the putative catalytic triad. CARB preferentially hydrolysed acyl chains with eight carbon atoms, and its activity was optimal at a pH of 7Á0 and a temperature of 25°C. CARB exhibited stability in alkaline pH, high activity under mesophilic conditions and stability in organic solvents. Conclusion: The CARB protein is potentially useful in bioremediation, food and chemical/pharmaceutical industries. Significance and Impact of the Study: This study is the first to report the development of a recombinant strain superproducing a Penicillium sp. carboxylesterase.

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“…The common limitation of industrial application of lipases and esterases is their limited thermostability at high temperatures and pH stability in operating industrial conditions. Therefore, searching for the novel microbial enzyme sources is of great importance in the development of new thermostable enzymes and applications [7,8].…”

Section: Introductionmentioning

confidence: 99%

Characterization of an extracellular thermophilic alkaline esterase produced by Bacillus subtilis DR8806

Asoodeh

Ghanbari

2013

Journal of Molecular Catalysis B: Enzymatic

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Determination and Characterization of Thermostable Esterolytic Activity from a Novel Thermophilic Bacterium Anoxybacillus gonensis A4

Cited by 32 publications

References 30 publications

A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: An extremely thermo- and pH-stable esterase

A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: An extremely thermo- and pH-stable esterase

Carboxyl ester hydrolase from Penicillium expansum : cloning, characterization and overproduction by Penicillium griseoroseum

Characterization of an extracellular thermophilic alkaline esterase produced by Bacillus subtilis DR8806

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