Yıl 2013, Cilt 37, Sayı 5, Sayfalar 538 - 546 2014-05-16

Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38
Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38

Aysun ADAN GÖKBULUT [1] , Alper ARSLANOĞLU [2]

174 338

An extracellular lipase producing bacterium was isolated from a soil sample, and identified as a strain of Pseudomonas fluorescens by 16S rRNA gene sequencing. It was named Pseudomonas fluorescens KE38. KE38 showed psychrotolerant properties with an optimum growth temperature of 25 °C. The lipase enzyme secreted by KE38 was purified 41.13-fold with an overall yield of 54.99%, and a specific activity of 337.3 U/mg. The molecular mass of purified lipase was estimated to be approximately 43 kDa by SDS-PAGE. Although the lipase was active at a temperature range of 15–65 °C, it exhibited maximum activity at 45 °C, at pH 8.0. The enzyme exhibited high stability retaining 100% and 70% of its activity after an incubation period of 45 and 100 min at 45 °C and pH 8.0 respectively. It also showed a broad substrate specificity acting on p-nitrophenyl esters with C8-C18 acyl groups as substrates and was activated by Ca2+ and Ni2+ at 1 mM. While the enzyme retained its activity levels in the presence of a variety of organic solvents, DMSO and dimethylformamide enhanced this. High stability, broad substrate specificity and activity at cold temperatures in the presence of organic solvents, and metal ions make the extracellular lipase of KE38 a candidate for industrial applications.
An extracellular lipase producing bacterium was isolated from a soil sample, and identified as a strain of Pseudomonas fluorescens by 16S rRNA gene sequencing. It was named Pseudomonas fluorescens KE38. KE38 showed psychrotolerant properties with an optimum growth temperature of 25 °C. The lipase enzyme secreted by KE38 was purified 41.13-fold with an overall yield of 54.99%, and a specific activity of 337.3 U/mg. The molecular mass of purified lipase was estimated to be approximately 43 kDa by SDS-PAGE. Although the lipase was active at a temperature range of 15–65 °C, it exhibited maximum activity at 45 °C, at pH 8.0. The enzyme exhibited high stability retaining 100% and 70% of its activity after an incubation period of 45 and 100 min at 45 °C and pH 8.0 respectively. It also showed a broad substrate specificity acting on p-nitrophenyl esters with C8-C18 acyl groups as substrates and was activated by Ca2+ and Ni2+ at 1 mM. While the enzyme retained its activity levels in the presence of a variety of organic solvents, DMSO and dimethylformamide enhanced this. High stability, broad substrate specificity and activity at cold temperatures in the presence of organic solvents, and metal ions make the extracellular lipase of KE38 a candidate for industrial applications.
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Yazar: Aysun ADAN GÖKBULUT
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Yazar: Alper ARSLANOĞLU
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Bibtex @ { tbtkbiology139558, journal = {Turkish Journal of Biology}, issn = {1300-0152}, address = {TÜBİTAK}, year = {2014}, volume = {37}, pages = {538 - 546}, doi = {10.3906/biy-1211-10}, title = {Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38}, key = {cite}, author = {GÖKBULUT, Aysun ADAN and ARSLANOĞLU, Alper} }
APA GÖKBULUT, A , ARSLANOĞLU, A . (2014). Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38. Turkish Journal of Biology, 37 (5), 538-546. DOI: 10.3906/biy-1211-10
MLA GÖKBULUT, A , ARSLANOĞLU, A . "Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38". Turkish Journal of Biology 37 (2014): 538-546 <http://dergipark.gov.tr/tbtkbiology/issue/11690/139558>
Chicago GÖKBULUT, A , ARSLANOĞLU, A . "Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38". Turkish Journal of Biology 37 (2014): 538-546
RIS TY - JOUR T1 - Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38 AU - Aysun ADAN GÖKBULUT , Alper ARSLANOĞLU Y1 - 2014 PY - 2014 N1 - doi: 10.3906/biy-1211-10 DO - 10.3906/biy-1211-10 T2 - Turkish Journal of Biology JF - Journal JO - JOR SP - 538 EP - 546 VL - 37 IS - 5 SN - 1300-0152-1303-6092 M3 - doi: 10.3906/biy-1211-10 UR - http://dx.doi.org/10.3906/biy-1211-10 Y2 - 2018 ER -
EndNote %0 Turkish Journal of Biology Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38 %A Aysun ADAN GÖKBULUT , Alper ARSLANOĞLU %T Purification and biochemical characterization of an extracellular lipase from psychrotolerant Pseudomonas fluorescens KE38 %D 2014 %J Turkish Journal of Biology %P 1300-0152-1303-6092 %V 37 %N 5 %R doi: 10.3906/biy-1211-10 %U 10.3906/biy-1211-10