Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeonSulfolobus solfataricus

Chung, Young Mi; Park, Chan B.; Lee, Sun Bok

doi:10.1007/bf02932354

Cited by 7 publications

(3 citation statements)

References 9 publications

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“…The temperature profile of PPL showed that the enzyme has the optimum temperature at 37 • C and its activity was drastically reduced at 50 • C, thus the half-life was only assessed at 37 • C. The data indicated that the PPL shows the half-life of 105 min at 37 • C (data not shown). The optimum temperature of the isolated enzyme was as same as lipase from Pseudozyma hubeiensis strain HB85A [35] and Talaromyces thermophilus [8], but less than esterases from T. thermophilus HB27 (80 • C at pH 8) [27], Anoxybacillus gonensis G2 (60 • C at pH 7.5) [36], Sulfolobus solfataricus (75 • C at pH 8) [37].…”

Section: Enzyme Characterizationmentioning

confidence: 99%

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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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Section: Enzyme Characterizationmentioning

confidence: 99%

“…The bacteria were cultured for 34 h at three different temperatures (37,42, 50 • C). Our results indicated that the optimum growth (OD 600 nm) was at 50 • C and the maximum enzyme production was observed after 20 h of the incubation.…”

Section: Enzyme Productionmentioning

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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“…The neutral pH optimum was similar to those of some plant and microbial esterases from a thermoacidophilic archaeon, Thermotoga maritima, and Chrysosporium lucknowense C1 16−18 and pH 8.0 from Streptococcus thermophilus and Sulfolobus solfataricus. 19,20 The effect of temperature on esterase activity was studied in the range of 30 to 80 • C at pH 7.0. The optimum temperature for the enzyme was 50 • C and at least 70% of maximum activity was retained between 30 and 70 • C, while 70% of maximum activity was lost at 80 • C (Figure 3B).…”

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 99%

Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Özbek¹,

Kolcuoğlu²,

Konak³

et al. 2014

Turk J Chem

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An esterase from a thermophilic bacterium, Geobacillus sp. DF20, was partially purified. Final purification factor was found to be 64.5-fold using Q-Sepharose ion exchange column chromatography. Native polyacrylamide gel electrophoresis indicated the presence of a single active esterase. The substrate specificity of this esterase was high for p -nitrophenyl butyrate ( p NPB) substrate. The optimum pH and temperature for the enzyme activity were 7.0 and 50• C, respectively. The pH and heat stability profiles show that this enzyme is more stable under neutral conditions at 50• C. Km and Vmax values for this esterase acting on p NPB were 0.12 mM and 54.6 U/mg protein, respectively.Presence of 10% (v/v) acetonitrile in the reaction medium indicated that purified enzyme was strongly inhibited. It was also detected that some metal ions affected enzyme activity at different rates. As a result, it was observed that esterase from Geobacillus sp. DF20 has extreme temperature and pH stabilities. Therefore, the stability and Km value of the enzyme make this study interesting when compared with the literature.

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Purification and characterization of a highly thermostable esterase from the actinobacterium Geodermatophilus obscurus strain G20

Jaouani

Neifar

Hamza

et al. 2012

J. Basic Microbiol.

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Intracellular thermostable esterase produced by the extremophilic Geodermatophilus obscurus G20 was purified to homogeneity by a heat treatment, followed by an anion-exchange chromatography, and then characterized. The molecular weight of the purified enzyme determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was shown to be approximatively 55 kDa. The enzyme showed an optimal activity between pH 8.0 and 9.0 and was stable in the pH range 7.0-10.0. Moreover, it is highly thermostable, with a residual activity greater than 90% after incubation at 80 °C for more than 10 h. The enzyme showed preference for esters of p -nitrophenol with short chain fatty acid. When the p -nitrophenyl acetate (C2) was used as substrate, the Michaelis-Menten constant (K(m) ) and maximum velocity for the reaction (V(max) ) of esterase were 400 μM and 2500 U/mg protein, respectively. The effect of phenylmethanesulphonyl fluoride (PMSF), a serine-specific inhibitor, on the enzyme activity suggested that the thermostable esterase belong to the serine hydrolase group. Because of its high thermostability, activity at alkaline pH, tolerance to methanol and various metal ions and specificity for short chain fatty acids, this enzyme showed high potential for use in biocatalysis. (© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim).

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Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeonSulfolobus solfataricus

Cited by 7 publications

References 9 publications

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

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

Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Purification and characterization of a highly thermostable esterase from the actinobacterium Geodermatophilus obscurus strain G20

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