Optimization of culture conditions for production of lipase by a newly isolated bacterium Stenotrophomonas maltophilia

Hasan-Beikdashti, Morvarid; Forootanfar, Hamid; Safiarian, Mohammad S.; Ameri, Atefeh; Ghahremani, Mohammad Hossein; Khoshayand, Mohammad Reza; Faramarzi, Mohammad Ali

doi:10.1016/j.jtice.2012.03.005

Cited by 76 publications

(46 citation statements)

References 37 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%

“…In addition, salt and thermal tolerance assays were performed by cultivating the selected isolate in the BHI agar medium containing different concentrations of NaCl (0-20%) and temperatures (5-75°C), respectively. Further identification of the selected isolate was done by 16S rDNA gene sequence analysis method after amplification of the desired gene using the forward primer 27F (5'-AGAG TTTGATCCTGGCTCAG-3') and the reverse primer 1525R (5'-AAGGAGGTGATCCAGCC-3') (Hasan-Beikdashti et al, 2012;Forootanfar et al, 2014). The amplified DNA fragment was consequently purified from 1% agarose gel and sent for automated sequencing (Bioneer, South Korea) using the above mentioned primers.…”

Section: Methodsmentioning

confidence: 99%

“…The selected isolate was cultivated at 60°C and 120 rpm for 72 h in the 500 mL Erlenmyer flasks containing 150 mL of basal medium including 10 g LG 1 olive oil, 5 mannose 200 g LG 1 NaCl, 2 g LG 1 (NH 4 ) 3 PO 4 , 2 g LG 1 NaH 2 PO 4 , 2 g LG 1 NaNO 3 and 0.04 g LG 1 FeSO 4 .7H 2 O. Interval samples were taken and the OD 600 was determined after decanting the remained olive oil (Hasan-Beikdashti et al, 2012). Lipase activity of the obtained supernatant (after removing bacterial cell using centrifugation at 10000 g for 10 min) was measured as described in the next section.…”

Section: Media and Culture Conditionsmentioning

confidence: 99%

“…Assay for lipase activity and protein estimation: Activity of the lipase was determined spectrophotometrically using ρ-NPP as substrate according to the method described by Hasan-Beikdashti et al (2012) with some modifications. The reaction mixture including 0.8 mL of 0.1 M phosphate buffer (pH 7.8) containing 0.4% of Triton X-100, 0.1 mL of the freshly prepared ρ-NPP solution (0.01 M) and 0.1 mL of taken supernatant sample was incubated at 60°C and 120 rpm for 30 min.…”

Section: Media and Culture Conditionsmentioning

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: Methodsmentioning

confidence: 99%

Section: Media and Culture Conditionsmentioning

confidence: 99%

Section: Media and Culture Conditionsmentioning

confidence: 99%

See 2 more Smart Citations

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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show abstract

“…(Gupta et al 2007), Stenotrophomonas sp. (Hasan-Beikdashti et al 2012), etc., are noteworthy among them. Box-Behnken and central composite designs of RSM have been applied in the above cases.…”

Section: The Use Of Statistical Tools For Optimizing Lipase Productionmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

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Laccase and Laccase‐Mediated Systems in the Synthesis of Organic Compounds

2014

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Laccase, a blue multicopper oxidase, has recently received considerable attention because of its usefulness in oxidizing phenolic and non‐phenolic compounds, as well as its suitability for organic synthesis, environmental pollutant treatment, and other biotechnological applications. This review covers recent studies on the structural properties, occurrence, reaction mechnisms, redox mediators of laccases and their application in organic synthesis procedures, such as dimerization, polymerization, oxidation, and amination. We also present a brief discussion on laccase activity in non‐aqueous media. Given that the development of green protocols for the synthesis of pure compounds is one of the main goals of sustainable chemistry, the exploitation of laccases is expected to remain one of the most popular directions in future biocatalysis research.magnified image

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Optimization of culture conditions for production of lipase by a newly isolated bacterium Stenotrophomonas maltophilia

Cited by 76 publications

References 37 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

An insight into microbial lipases and their environmental facet

Laccase and Laccase‐Mediated Systems in the Synthesis of Organic Compounds

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