Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt

Soliman, Nadia A.; Knöll, Martin; Abdel-Fattah, Yasser R.; Schmid, Rolf D.; Lange, Stefan

doi:10.1016/j.procbio.2007.05.005

Cited by 92 publications

(74 citation statements)

References 46 publications

(57 reference statements)

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“…3). Similar results have been demonstrated by other studies (Soliman et al 2007;Yildirim et al 2009;MontoroGarcía et al 2009) having the highest esterase activity toward p-nitrophenyl acetate. The results were not surprising because esterase use short chain fatty acids as substrate for their catalytic activity.…”

Section: Resultssupporting

confidence: 91%

“…The recombinant esterases were very stable when held at pH 9.5-11.0 for hours, retaining 80-100% of its initial activity (data is not shown) indicating that the recombinant enzymes are extremely alkali-tolerant proteins. Similar to the results here, esterase enzyme from G. thermoleovorans and B. subtilis have been reported to be more active and stable at alkaline pH (Eggert et al 2000;Soliman et al 2007). This is in fact a desirable property for industrial applications.…”

Section: ; Soliman Et Al 2007) Having the Highest Activity With supporting

confidence: 89%

“…4a). Similar results were also reported for esterases from G. thermoleovorans YN, G. stearothermophilus and G. caldoxylosilyticus TK4 (Soliman et al 2007;Yildirim et al 2009;Ewis et al 2004). Although the enzymes have exhibited similar activity trend with increased temperature, their activities were slightly different at lower and higher temperature.…”

Section: ; Soliman Et Al 2007) Having the Highest Activity With supporting

confidence: 85%

“…subtilis str. 168, respectively (Ewis et al 2004;MontoroGarcía et al 2009;Soliman et al 2007, Kneusel et al 1994). …”

Section: Resultsunclassified

“…However, incubation at temperatures above 75°C for more than 60 min resulted in a rapid inactivation of enzymes and lost almost all activities after 3 h. High thermostability has been shown with other homologous enzymes from G. thermoleovorans, G. stearothermophilus, Geobacillus sp. and G. kaustophilus HTA426 (Soliman et al 2007;Owsu and Cowan 1991;Janssen et al 1994;Montoro-García et al 2009). Fig.…”

Section: ; Soliman Et Al 2007) Having the Highest Activity With mentioning

confidence: 99%

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Molecular cloning, over expression and characterization of thermoalkalophilic esterases isolated from Geobacillus sp.

Tekedar

Şanlı‐Mohamed

2010

Extremophiles

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Due to potential use for variety of biotechnological applications, genes encoding thermoalkalophilic esterase from three different Geobacillus strains isolated from thermal environmental samples in Balçova (Agamemnon) geothermal site were cloned and respective proteins were expressed in Escherichia coli (E.coli) and characterized in detail. Three esterases (Est1, Est2, Est3) were cloned directly by PCR amplification using consensus degenerate primers from genomic DNA of the strains Est1, Est2 and Est3 which were from mud, reinjection water and uncontrolled thermal leak, respectively. The genes contained an open reading frame (ORF) consisting of 741 bp for Est1 and Est2, which encoded 246 amino acids and ORF of Est3 was 729 bp encoded 242 amino acids. The esterase genes were expressed in E. coli and purified using His-Select HF nickel affinity gel. The molecular mass of the recombinant enzyme for each esterase was approximately 27.5 kDa. The three esterases showed high specific activity toward short chain p-NP esters. Recombinant Est1, Est2, Est3 have exhibited similar activity and the highest esterase activity of 1,100 U/mg with p-nitrophenyl acetate (pNPC 2 ) as substrate was observed with Est1. All three esterase were most active around 65°C and pH 9.5-10.0. The effect of organic solvents, several metal ions, inhibitors and detergents on enzyme activity for purified Est1, Est2, Est3 were determined separately and compared.

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Section: Resultssupporting

confidence: 91%

Section: ; Soliman Et Al 2007) Having the Highest Activity With supporting

confidence: 89%

Section: ; Soliman Et Al 2007) Having the Highest Activity With supporting

confidence: 85%

“…subtilis str. 168, respectively (Ewis et al 2004;MontoroGarcía et al 2009;Soliman et al 2007, Kneusel et al 1994). …”

Section: Resultsunclassified

Section: ; Soliman Et Al 2007) Having the Highest Activity With mentioning

confidence: 99%

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Molecular cloning, over expression and characterization of thermoalkalophilic esterases isolated from Geobacillus sp.

Tekedar

Şanlı‐Mohamed

2010

Extremophiles

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Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

Wang

Zhang

et al. 2018

Chirality

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The two enantiomers of ethyl 3-hydroxybutyrate are important intermediates for the synthesis of a great variety of valuable chiral drugs. The preparation of chiral drug intermediates through kinetic resolution reactions catalyzed by esterases/lipases has been demonstrated to be an efficient and environmentally friendly method. We previously functionally characterized microbial esterase PHE21 and used PHE21 as a biocatalyst to generate optically pure ethyl (S)-3-hydroxybutyrate. Herein, we also functionally characterized one novel salt-tolerant microbial esterase WDEst17 from the genome of Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085. Esterase WDEst17 was further developed as an efficient biocatalyst to generate (R)-3-hydroxybutyrate, an important chiral drug intermediate, with the enantiomeric excess being 99% and the conversion rate being 65.05%, respectively, after process optimization. Notably, the enantio-selectivity of esterase WDEst17 was opposite than that of esterase PHE21. The identification of esterases WDEst17 and PHE21 through genome mining of microorganisms provides useful biocatalysts for the preparation of valuable chiral drug intermediates.

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pH‐Profiling of thermoactive lipases and esterases: Caveats and further notes

Hriscu

Chiş

Toşa

et al. 2013

Euro J Lipid Sci & Tech

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A common technique for assaying lipase/esterase activity in vitro is the enzymatic cleavage of para-nitrophenyl esters, with spectrophotometric monitorization at 405-410 nm of the released p-nitrophenol ( pNP). This method has its limitations, since the extinction coefficient of pNP is strongly pH-dependent. Despite this, the method is being frequently used for investigating lipolytic activity over a pH range without any pH-related corrections, which may bring along false results. We show to what extent the results may be altered by this approach and we review alternative strategies allowing the method to become usable both in the acidic range and with varying pH.

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Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt

Cited by 92 publications

References 46 publications

Molecular cloning, over expression and characterization of thermoalkalophilic esterases isolated from Geobacillus sp.

Molecular cloning, over expression and characterization of thermoalkalophilic esterases isolated from Geobacillus sp.

Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

pH‐Profiling of thermoactive lipases and esterases: Caveats and further notes

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