A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains

Kademi, Ali; Ait-Abdelkader, Nadra; Fakhreddine, Loubna; Baratti, J.

doi:10.1016/s0141-0229(98)00127-6

Cited by 43 publications

(27 citation statements)

References 37 publications

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“…Uncommonly some activity toward PNP-palmitate (C16 acyl group) was detected. The same was found in case of an esterase from a newly isolated moderate thermophilic bacterium (Kademi et al 1999) and another esterases from G. thermoleovorans YN and G. kaustophilus HTA426 (Montoro-García et al…”

Section: Resultssupporting

confidence: 67%

“…Unfortunately esterases are used less frequently in industrial processes compared to lipases mainly due to their lack of availability (Bornscheuer 2002;Faber 1997). Up to date, several thermostable lipases have been reported from thermophilic microorganisms (AbdelFattah and Gaballa 2006;Rua et al 1997;Schmidt-Dannert et al 1996;Kim et al 1998;Margolin 1993), whereas only few thermostable esterases have been isolated from thermophile microorganisms in the literature (Ewis et al 2004;Kademi et al 1999;Mnisi et al 2005).…”

Section: Introductionmentioning

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: 67%

Section: Introductionmentioning

confidence: 99%

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

Tekedar

Şanlı‐Mohamed

2010

Extremophiles

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“…After 40 h of cultivation at pH 6.5, a maximum of 0.36 U/mL lipase activity was produced by B. thermocatenulatus [5]. Finally, Bacillus circulans showed a maximum lipase activity of only 0.04 U/mL [2].…”

Section: Lipid Degradationmentioning

confidence: 99%

“…It has been reported that enzyme resistance to denaturation in organic solvents is correlated with their thermostability in water. For this reason, thermostable enzymes are attractive not only to be used in aqueous media but also in organic media [2].…”

Section: Introductionmentioning

confidence: 99%

“…The few lipases produced by thermophilic bacterial isolates reported in the recent literature include mainly bacilli species such as Bacillus thermoleovorans IHI-91 [3]; Bacillus thermoleovorans ID-1 [4]; Bacillus thermocatenulatus [5] and Bacillus circulans [2]. Only one study reported on a lipase produced by an actinomycete, Thermoactinomyces vulgaris [6].…”

Section: Introductionmentioning

confidence: 99%

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A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

Al-Khudary

Hashwa²,

Mroueh

2004

Engineering in Life Sciences

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A filamentous, Gram-positive, spore forming aerobic bacterium was isolated from olive oil contaminated soil (Al Koura, Lebanon) on rhodamine agar plates at 60 C. The isolate, HRK-1 produced large quantities of an extracellular thermostable lipase which degrades olive oil. It was primarily classified as a Thermoactinomyces sp. due to the filamentous structure of its cells that bear one spore each on an un-branched sporophore, the resistance of its spores to boiling, utilisation of sucrose as a carbon source and production of dark pigments. The isolate grew optimally at a temperature of 60 C, a pH of 7.3 and an orbital shaking of 250 rpm. It showed an efficient olive oil degrading ability. No traces of triolein were detected after a 36-h cultivation. A concentration of 10 % [v/v] olive oil did not inhibit its growth. Lipase production was constitutive, and did not depend on the presence of olive oil. The optimum concentration of olive oil for lipase activity was 1 % [v/v], and the activity was not enhanced at higher concentrations, but on the contrary, a decrease in enzyme activity was recorded. The lipase of HRK-1 was preliminarily characterised in the crude cell-free supernatant with a specific activity of 0.14 U/mg. It has an optimum activity at 60 C and a pH of 8.0. This lipolytic enzyme showed resistance to boiling and to a wide range of metallic ions and inhibitors. The formation of this heat-stable lipase started in the early exponential growth phase, while a maximum extracellular enzyme activity was detected at the end of the decline phase, when most of the cells appeared as spherical spores. The exceptionally high activity of lipase (2.37 U/ml) produced by HRK-1 measured in the cell free supernatant clearly indicated the commercial importance of this isolate, especially after it showed great stability at elevated temperatures.

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Enhanced thermostability of the immobilized thermoalkalophilic esterase onto magnetic‐cornstarch nanoparticle

Öz

Sürmeli

Şanlı‐Mohamed

2021

Biotech and App Biochem

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The immobilization of the biocatalysts onto magnetic nanoparticles has been extensively applied as the external magnetic field facilitates the enzyme recovery from the reaction mixture. In the present study, glutaraldehyde‐modified magnetite‐cornstarch nanoparticles (MCNs) were successfully synthesized, elaborately characterized by ZetaSizer and surface‐enhanced Raman spectroscopy, and used for the immobilization of a thermoalkalophilic esterase from Geobacillus sp. The optimal immobilization conditions were obtained at 65°C, 2:3 molar ratios of Fe2+:Fe3+, and 1 g cornstarch resulted in approximately 90 nm magnetic particles in size. Also, immobilization yield and immobilization efficiency of the esterase were found as 74% and 82%, respectively. Scanning electron microscopy micrographs showed that MCNs were uniform, spherical in shape, and well dispersed and esterase immobilized MCNs displayed similar morphology as free MCNs. The maximum activity of free and immobilized esterase was obtained at 65°C and pH 9. Immobilization onto glutaraldehyde‐modified MCNs significantly enhanced the esterase thermostability. Additionally, the immobilized esterase kept its residual activity of 75% after three sequential cycles, suggesting that it has favorable operational stability.

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A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains

Cited by 43 publications

References 37 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.

A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

Enhanced thermostability of the immobilized thermoalkalophilic esterase onto magnetic‐cornstarch nanoparticle

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