Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase

Daoud, Lobna; Kamoun, Jannet; Ali, Madiha Bou; Jallouli, Raida; Bradai, Rim; Mechichi, Tahar; Gargouri, Youssef; Ali, Yassine Ben; Aloulou, Ahmed

doi:10.1016/j.ijbiomac.2013.03.018

Cited by 39 publications

(26 citation statements)

References 34 publications

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“…Thereafter, 500 µL of each obtained filtrate was spread on a BHI agar plate containing Rhodamine B (0.001%, w/v), olive oil (1%, v/v) and NaCl (15% w/v). The culture plates were then incubated at 60°C and the colonies harboring orange fluorescence halos around them (under ultraviolet light of 350 nm) were regarded as the lipase producer (Hasan-Beikdashti et al, 2012;Daoud et al, 2013). The most potent lipase producing isolates were re-isolated for several times to confirm their purity and then conserved in glycerol 20% (v/v) at -80°C.…”

Section: Methodsmentioning

confidence: 99%

“…These valuable biocatalysts have been widely used in various industries such as food (for example, hydrolysis of milk fat and cheese ripening in dairy foods), detergent, pulp and paper (papers with improved quality), fine chemicals (such as resolution of racemic acids and alcohols and regioselective acylations) and oleochemical manufacturing (Salameh and Wiegel, 2007;Sharma et al, 2011;AbdelFattah et al, 2012). Synthesis of biopolymers and biodiesel, resolution of enantio-specific pharmaceuticals and production of agro-chemicals and flavoring compounds are among other biotechnological applications of lipases (Soliman et al, 2007;Yu et al, 2010;Andualema and Gessesse, 2012 [154][155][156][157][158][159][160][161][162][163][164]2015 Because of high demands for the lipases tolerant to extreme conditions, screening of the environments harboring halophilic and thermophilic lipase-producing microbial strains is still a main step for introducing lipolytic enzyme with remarkable properties (Daoud et al, 2013;Masomian et al, 2013). Extremophiles include microorganisms which are able to survive in harsh environmental conditions, such as extremely high or low temperatures, high concentration of salt, severe alkaline or acidic pH, low water activity and high pressure (Salameh and Wiegel, 2007;Moshfegh et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…There are many reports on the production of lipases originated from exteremophiles such as Burkholderia ambifaria YCJ01 (Yao et al, 2013), Fervidobacterium nodosum Rt17-B1 (Yu et al, 2010), Staphylococcus xylosus (Bouaziz et al, 2011), Staphylococcus sp. (Daoud et al, 2013) and Aneurinibacillus thermoaerophilus strain HZ. (Masomian et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Ameri¹,

Shakibaie²,

Amirpour-R³

et al. 2015

Biotechnology

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A B S T R A C T A thermoalkalophilic lipase producing bacterial strain, identified asBacillus atrophaeus FSHM2 using 16S rDNA sequencing analysis was isolated from salty soil and its lipase was partially purified and characterized. The obtained results revealed that glucose, hazelnut oil, urea and calcium ion positively affected the lipase production by increasing the lipolytic activity to 13582.5, 6270, 4442 and 5505 U LG 1 , respectively compared to that of basal medium (4150 U LG 1 ). The partially purified lipase acted optimally at pH 9 and retained 88.2% of its initial activity after 1 h of incubation at 100°C. A two fold increase in the relative activity of the partially purified lipase was obtained in the presence of 4 M of NaCl. Application of the partially purified lipase for the synthesis of ethyl and methyl valerate in the organic solvent medium (xylene) resulted in 81.6 and 62.4% esterification, respectively, after 24 h of incubation.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Ameri¹,

Shakibaie²,

Amirpour-R³

et al. 2015

Biotechnology

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“…Halophilic microorganisms have the ability to adapt to high salt concentrations by balancing the osmotic pressure of their cytoplasm. Hypersaline media leads to protein aggregation by forming electrostatic interactions between the bonds of protein, but the halophilic proteins maintain their three-dimensional structure and conserve their activities in such environments 19 . Several lipolytic enzymes have been reported which are active and stable in extreme conditions such as hypersalinity…”

Section: -21mentioning

confidence: 99%

“…These results are similar to the results of a halotolerant Staphylococcus spp. extracellular lipase which was characterized by Daoud et al (2013) 19 . Extracellular lipase of this strain showed optimal activity at pH 8.0…”

Section: Effect Of Temperature Ph and Nacl Concentration On Enzyme Amentioning

confidence: 99%

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

Ozgen

Attar

Elalmış

et al. 2016

Polish Journal of Chemical Technology

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A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2 were determined. It was observed that the lipolytic activity of Haloarcula hispanica was stimulated by some of the carbon sources. The high lipase acitivity values were obtained in the presence of 2% (v/v) walnut oil (6.16 U/ml), 1% (v/v) fi sh oil (5.07 U/ml), 1% (v/v) olive oil (4.52 U/ml) and 1% (w/v) stearic acid (4.88 U/ml) at 4M NaCl concentration. Lipase was partially purifi ed by ammonium sulfate precipitation and ultrafi ltration. Optimal temperature and pH values were determined as 45 o C and 8.0, respectively. Lipase activity decreased with the increasing salt concentration, but 85% activity of the enzyme was maintained at 5M NaCl concentration. The enzyme preserved 41% of its relative activity at 90 o C. The partially purifi ed lipase maintained its activity in the presence of surfactants such as Triton X-100 and SDS. Therefore, the lipase which is an extremozyme may have potential applications especially in detergent industry.

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An organic solvent‐stable lipase from a newly isolated Staphylococcus aureus ALA1 strain with potential for use as an industrial biocatalyst

Bacha

Moubayed

Al-Assaf

2015

Biotech and App Biochem

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In this study, a new strain, ALA1, was identified as Staphylococcus aureus by biochemical tests, and its 16S ribosomal DNA sequence was isolated from dromedary milk. ALA1 lipase production was optimized in shake flask experiments and measured with varying pH (3-11), temperature (20-55 °C) and substrate concentrations. The maximum lipase production was recorded at pH 8 and 30 °C for up to 30 H of culture period for the S. aureus ALA1 strain. Among the substrates tested, selected carbon sources, xylose, nitrogen source, yeast extract, and olive oil (1%) were suitable for maximizing lipase production. The effects of surfactants were investigated and showed that Tween 20, Tween 80, and Triton X-100 prevented lipase production. Interestingly, isolate ALA1 was able to grow in high concentrations of benzene or toluene (up to 50% (v/v)). Moreover, the lipolytic activity of the S. aureus ALA1 lipase was stimulated by diethyl ether, whereas almost 100% of S. aureus ALA1 lipase activity was retained in 25% acetone, acetonitrile, benzene, 2-propanol, ethanol, methanol, or toluene. Because of its stability in organic solvent, the S. aureus ALA1 lipase was used as a biocatalyst to synthesize high levels of added value molecules. S. aureus ALA1 lipase could be considered as an ideal choice for applications in detergent formulations because of its high stability and compatibility with various surfactants, oxidizing agents, and commercial detergents.

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Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase

Cited by 39 publications

References 34 publications

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

An organic solvent‐stable lipase from a newly isolated Staphylococcus aureus ALA1 strain with potential for use as an industrial biocatalyst

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