Diphenolases from Anoxybacillus kestanbolensis strains K1 and K4 T

Yildirim, Melike; Col, Melek; Çolak, Ahmėt; Güner, Saaclettin; Dülger, Sabriye; Beldüz, Ali Osman

doi:10.1007/s11274-004-2392-0

Cited by 18 publications

(9 citation statements)

References 35 publications

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“…The residual activity was determined in standard conditions using PNPA as substrate. The percentage residual esterase activity was calculated by comparison with unincubated enzyme at the optimum conditions (Yildirim et al. 2005).…”

Section: Methodsmentioning

confidence: 99%

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

Çolak

Camedan

Faiz

et al. 2009

Journal of Food Biochemistry

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Lycoperdon perlatum Pers. (Lycoperdaceae, Agaricales, Agaricomycetidae, Agaricomycetes, Basidiomycota, Fungi) was evaluated for its esterolytic potential. Native electrophoresis of the crude extracts showed four bands having Rf values of 0.34, 0.39, 0.52 and 0.59. The esterase showed the highest activity toward a short‐chain substrate, p‐nitrophenyl acetate. Optimum reaction conditions for L. perlatum crude extract were attained at pH 8.0 and 40C. Esterolytic activity of enzyme extract was stimulated in the presence of Mn2+, Fe2+, Ca2+ and Zn2+ in the reaction mixture. The enzyme activity was stimulated by incubation at pH 6.0 but retained 77% of its original activity at its optimum pH after 24 h. Thermal inactivation was displayed after incubation for 20 min at various temperatures above 30C. At 1 mM final concentration, 2‐mercaptoethanol, dithiothreitol, ethylenediamine tetraacetic acid and p‐methylphenyl sulfonylfluoride inhibited the esterolytic reaction. These results support that the crude L. perlatum extract possesses an esterolytic activity having properties similar to other esterases. PRACTICAL APPLICATIONS Esterases catalyzing the cleavage and formation of ester bonds are known α/β‐hydrolases (EC 3.1.1.X). Esterases are used for the synthesis of flavor esters for the food industry, modification of triglycerides for fat and oil industry and resolution of racemic mixtures used for the synthesis of fine chemicals for the pharmaceutical industry. Therefore, the search for new enzyme sources is important for the development of new enzymes and applications.

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Section: Methodsmentioning

confidence: 99%

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

Çolak

Camedan

Faiz

et al. 2009

Journal of Food Biochemistry

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“…After reaching to room temperature, the esterase activity was determined at standard assay conditions. Control with non-incubated enzyme was used to determine the 100% activity value [28].…”

Section: Ph-and Thermal-stability Of the Enzymementioning

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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“…At the end of the storage period, the esterase activity was assayed under standard reaction conditions. The percentage residual enzyme activity was calculated by comparison with nonincubated enzyme (Yildirim et al . 2005).…”

Section: Methodsmentioning

confidence: 99%

CHARACTERIZATION OF AN ESTERASE ACTIVITY INLYCOPERDON PYRIFORME, AN EDIBLE MUSHROOM

Akatin¹,

Çolak²,

Ertunga³

2011

Journal of Food Biochemistry

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An esterase from Lycoperdon pyriforme was characterized. The enzyme had a maximum activity at pH 8.0 and 40C with p‐nitrophenyl acetate as a substrate. Km and Vmax values were calculated as 2.13 mM and 0.65 U/mg protein, respectively. The enzyme activity was conserved more than 90% over a broad range of pH (3.0–9.0) at 4C after 24 h of incubation. The activity increased 37 ± 3.6% after 120 min of incubation at 40C. Li+, Mg2+ and Ca2+ activated the enzyme 12 ± 1.8, 16 ± 2.5 and 15 ± 2.5%, respectively. The esterase was inhibited in different ratios by some detergents such as Triton X‐114, Triton X‐100, Tween 20 (Sigma Chemical Co., St. Louis, MO) and sodium dodecylsulfate. It retained most of its activity in the presence of methanol and dimethylsulphoxide at the final concentration of 10% (v/v). pH and moderate thermal stability of L. pyriforme esterase and its activity in some organic solvents could make it useful for some industrial purposes such as detergent and paper industry. PRACTICAL APPLICATIONS Esterases play a major role in the degradation of natural materials and industrial pollutants, viz., cereal wastes, plastics and other toxic chemicals. They are also useful in the synthesis of optically pure compounds, perfumes and antioxidants. Because of these biocatalytic applications, it may be interesting to study novel esterases from different organisms. Therefore, it is important to study esterase activity of Lycoperdon pyriforme. In this way, a new esterase having potential applications can be found.

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Diphenolases from Anoxybacillus kestanbolensis strains K1 and K4 T

Cited by 18 publications

References 35 publications

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

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

CHARACTERIZATION OF AN ESTERASE ACTIVITY INLYCOPERDON PYRIFORME, AN EDIBLE MUSHROOM

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