Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Çolak, Ahmėt

doi:10.5505/tjb.2013.36035

Cited by 8 publications

(5 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, thermal denaturation of Pf_Est was accompanied by the measurement of the change in ellipticity at 221 nm over the temperature range of 20-100°C, showing that Pf_Est did not lose its secondary structure over this temperature range. These data reinforce the higher thermostability of Pf_Est when comparing to others previously described in the literature [36,39,42].…”

Section: Discussionsupporting

confidence: 91%

“…Pf_Est presented optimum pH activity at 6.5-7.0 in naphthol-derivate substrates, which is slightly lower than the optimum pH (7.5) reported earlier for esterases from Brevibacterium linens ATCC 9174, Thermus thermophilus HB27, and Geobacillus sp. TF17 [34][35][36]. The optimum temperature for Pf_Est activity was 80°C in a-naphthyl acetate (and butyrate) and 75°C in pNPP.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus

et al. 2016

View full text Add to dashboard Cite

Enzymes isolated from extremophiles often exhibit superior performance and potential industrial applications. There are several advantages performing biocatalysis at elevated temperatures, including enhanced reaction rates, increased substrate solubility and decreased risks of contamination. Furthermore, thermophilic enzymes usually exhibit high resistance against many organic solvents and detergents, and are also more resistant to proteolytic attack. In this study, we subcloned and characterized an esterase from the hyperthermophilic archaeon Pyrococcus furiosus (Pf_Est) that exhibits optimal activity around 80 °C using naphthol-derived substrates and p-nitrophenyl palmitate (pNPP). According to the circular dichroism spectra, the secondary structure of P. furiosus esterase, which is predominantly formed by a β-sheet structure, is very stable, even after incubation at 120°C. We performed SAXS to determine the low-resolution structure of Pf_Est, which is monomeric in solution at 80 °C and has a molecular weight of 28 kDa. The Km and V values for this esterase acting on pNPP were 0.53 mmol/L and 6.5 × 10 U, respectively. Pf_Est was most active in the immiscible solvents and retained more than 50 % in miscible solvents. Moreover, Pf_Est possesses transesterification capacity, presenting better results when isobutanol was used as an acyl acceptor (2.69 ± 0.14 × 10 μmol/min mg) and the highest hydrolytic activity toward olive oil among different types of oils testes in this study. Collectively, these biophysical and catalytic properties are of interest for several biotechnological applications that require harsh conditions, including high temperature and the presence of organic solvents.

show abstract

Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Carboxylesterases generally require no cofactor and exhibit high regiospecificity and stereospecificity due to the presence of a unique small acyl binding pocket, which optimally fits to the acyl moiety of their substrates (Panda & Gowrishankar, 2005). To date, thermostable carboxylesterases have been isolated and characterized from G. stearothermophilus ATCC12980 and ATCC7954 (Ewis, Abdelal, & Lu, 2004), G. thermoleovorans YN (Soliman, Abdel-Fattah, Mostafa, & Gaballa, 2014), G. thermodenitrificans T2 (Yang et al, 2013), G. thermodenitrificans CMB-A2 (Charbonneau, Meddeb-Mouelhi, & Beauregard, 2010), G. kaustophilus HTA426 (Montoro-García et al, 2009), G. caldoxylosilyticus TK4 (Yildirim, Colak, Col, & Canakci, 2009), G. thermoglucosidasius EAEC, and many other thermophilic strains attributed to the Geobacillus genus (Ayna, 2013;€ Ozbek, Kolcuo glu, Konak, Colak, & € Oz, 2014;Tekedar & Şanlı-Mohamed, 2011;Zhu et al, 2012). p0345…”

Section: U N C O R R E C T E D P R O O Fmentioning

confidence: 99%

The Genus Geobacillus and Their Biotechnological Potential

Hussein

Lisowska

Leak

2015

Advances in Applied Microbiology

View full text Add to dashboard Cite

The genus Geobacillus comprises a group of Gram-positive thermophilic bacteria, including obligate aerobes, denitrifiers, and facultative anaerobes that can grow over a range of 45-75°C. Originally classified as group five Bacillus spp., strains of Bacillus stearothermophilus came to prominence as contaminants of canned food and soon became the organism of choice for comparative studies of metabolism and enzymology between mesophiles and thermophiles. More recently, their catabolic versatility, particularly in the degradation of hemicellulose and starch, and rapid growth rates have raised their profile as organisms with potential for second-generation (lignocellulosic) biorefineries for biofuel or chemical production. The continued development of genetic tools to facilitate both fundamental investigation and metabolic engineering is now helping to realize this potential, for both metabolite production and optimized catabolism. In addition, this catabolic versatility provides a range of useful thermostable enzymes for industrial application. A number of genome-sequencing projects have been completed or are underway allowing comparative studies. These reveal a significant amount of genome rearrangement within the genus, the presence of large genomic islands encompassing all the hemicellulose utilization genes and a genomic island incorporating a set of long chain alkane monooxygenase genes. With G+C contents of 45-55%, thermostability appears to derive in part from the ability to synthesize protamine and spermine, which can condense DNA and raise its Tm.

show abstract

“…The enzyme retained 74% activity at pH 4.0 and 55% activity at pH 11.0 aer 1 h of incubation at room temperature. Zhang et al, 63 Adıgüzel 64 and Ayna et al 65 also reported esterase enzymes which were active at pH range 4.0-8.0, 4.0-10.0 and 4.0 to 9.0, respectively.…”

Section: Discussionmentioning

confidence: 96%

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

et al. 2022

View full text Add to dashboard Cite

show abstract

Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Cited by 8 publications

References 40 publications

Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus

Characterization and Low-Resolution Structure of an Extremely Thermostable Esterase of Potential Biotechnological Interest from Pyrococcus furiosus

The Genus Geobacillus and Their Biotechnological Potential

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

Contact Info

Product

Resources

About