Production and stabilization of a solvent-tolerant alkaline lipase from Pseudomonas pseudoalcaligenes F-111

Lin, Shuen-Fuh

doi:10.1016/s0922-338x(97)86981-4

Cited by 39 publications

(34 citation statements)

References 31 publications

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“…roqueforti IAM7268. The lipase activity was not affected by Ca 2 + , Mg 2 + , Mn 2 + , Na + , K + , Cu 2 + , EDTA, p-chloro mercuribenzoic acid, and iodoacetate (Mase et al, 1995 (Lin et al, 1996). Metal chelators (EDTA, o-phenanthrolin) did not significantly affect the alkaline lipase activity (Lin et al, 1996).…”

Section: Thermostability Of Lipasementioning

confidence: 85%

“…Several other studies confirm enhanced lipase production when oils are used as enzyme inducers. Lin et al (1996) produced an alkaline lipase from P. pseudoalcaligenes F-111 in a medium that contained both olive oil (0.4%) and Triton X-100 (0.2%). The addition of Triton X-100 enhanced the alkaline lipase production by 50-fold compared to using olive oil alone.…”

Section: Effect Of Carbon Sourcesmentioning

confidence: 99%

“…The extracellular lipase was measured using pNPP as the substrate (Vorderwiilbecke et al, 1992). Lin et al (1996) reported an extracellular alkaline lipase produced by P. alcaligenes F-111 in a medium that contained soybean meal (1%), peptone (1.5%), and yeast extract (0.5%). The lipase produced was unaffected by various detergents.…”

Section: Effect Of Nitrogen Sourcesmentioning

confidence: 99%

“…The purified lipase had a maximum hydrolytic activity at pH 10.0 and its molecular mass was 31 kDa by SDS-PAGE. Lin et al (1996) purified an alkaline lipase from P. pseudoalcaligenes F-111 to homogeneity. The apparent molecular mass by SDS-PAGE was 32 kDa and the isoelectric pH was 7.3 (Lin et al, 1996).…”

Section: Purification and Kinetic Characterization Of Lipasesmentioning

confidence: 99%

“…Lin et al (1996) purified an alkaline lipase from P. pseudoalcaligenes F-111 to homogeneity. The apparent molecular mass by SDS-PAGE was 32 kDa and the isoelectric pH was 7.3 (Lin et al, 1996). The enzyme showed a preference for C 12 aryl and C 14 acyl groups when using p-nitrophenyl esters as substrates.…”

Section: Purification and Kinetic Characterization Of Lipasesmentioning

confidence: 99%

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Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,271

712

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Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. The many applications of lipases include speciality organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses. This article discusses the production, recovery, and use of microbial lipases. Issues of enzyme kinetics, thermostability, and bioactivity are addressed. Production of recombinant lipases is detailed. Immobilized preparations of lipases are discussed. In view of the increasing understanding of lipases and their many applications in high-value syntheses and as bulk enzymes, these enzymes are having an increasing impact on bioprocessing. D

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Section: Thermostability Of Lipasementioning

confidence: 85%

Section: Effect Of Carbon Sourcesmentioning

confidence: 99%

Section: Effect Of Nitrogen Sourcesmentioning

confidence: 99%

Section: Purification and Kinetic Characterization Of Lipasesmentioning

confidence: 99%

Section: Purification and Kinetic Characterization Of Lipasesmentioning

confidence: 99%

See 3 more Smart Citations

Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,271

712

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Sequential parametric optimization of lipase production by a mutant strain Rhizopus sp. BTNT‐2

Bapiraju

Sujatha

Ellaiah

et al. 2005

J. Basic Microbiol.

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Lipase production by the mutant strain Rhizopus sp. BTNT-2 was optimized in submerged fermentation. Different chemical and physical parameters such as carbon sources, nitrogen sources, oils, inoculum level, pH, incubation time, incubation temperature and aeration have been extensively studied to increase lipase productivity. Potato starch (1.25% w/v) as a carbon source, corn steep liquor (1.5% w/v) as a nitrogen source and olive oil (0.5% v/v) as lipid source were found to be optimal for lipase production. The optimal levels of other parameters are 4 ml of inoculum (2.6x10(8) spores/ml), initial pH of 5.5, incubation time of 48 hours, incubation temperature of 28 degrees C and aeration rate of 120 rpm. With the optimized parameters, the highest production of lipase was 59.2 U/ml while an yield of only 28.7 U/ml was obtained before optimization resulting in 206% increase in the productivity.

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Characterization of an extracellular alkaline lipase from Pseudomonas mendocina M‐37

Dahiya

Arora

Chaudhury

et al. 2010

J. Basic Microbiol.

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A strain of Pseudomonas mendocina producing extracellular lipase was isolated from soil. The bacterium accumulates lipase in culture fluid when grown aerobically at 30 °C for 24 h in a medium composed of olive oil (1%) as substrate. Pseudomonas mendocina lipase was optimally active at pH 9.0, temperature of 50 °C and was found to be stable between pH 7.0-11.0. The lipase was inhibited by detergents such as SDS and Tween-80. The enzyme was stable in various organic solvents tested with maximum stability in chloroform followed by toluene and exhibited 1-3 regiospecificity for hydrolytic reaction. This lipase was capable of hydrolyzing a variety of lipidic substrates and is mainly active towards synthetic triglycerides and fatty acid esters that possess a butyryl group. Metal ions like Mg(2+), Ca(2+) and Na(+) stimulated lipase activity, whereas, Cu(2+), Mn(2+) and Hg(2+) ions caused inhibition.

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Production and stabilization of a solvent-tolerant alkaline lipase from Pseudomonas pseudoalcaligenes F-111

Cited by 39 publications

References 31 publications

Production, purification, characterization, and applications of lipases

Production, purification, characterization, and applications of lipases

Sequential parametric optimization of lipase production by a mutant strain Rhizopus sp. BTNT‐2

Characterization of an extracellular alkaline lipase from Pseudomonas mendocina M‐37

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