Properties of a thermostable and solvent stable extracellular lipase from aPseudomonas sp. AG-8

Sharma, Anil Kumar; Tiwari, Raj Gaurang; Hoondal, Gurinder Singh

doi:10.1002/1521-4028(200112)41:6<363::aid-jobm363>3.0.co;2-c

Cited by 29 publications

(12 citation statements)

References 14 publications

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“…The lipase from Pseudomonas sp. AG-8 was optimally active at 45 °C and the half life was 5 min at 70 °C (SHARMA et al 2001). Bacillus stearothermophilus L1 lipase was optimally active at 60 -65 °C (KIM et al 1998).…”

Section: Resultsmentioning

confidence: 97%

“…It retained more than 80% activity with Co 2+ , Ni 2+ and Pb 2+ and the activity was strongly inhibited by Cu 2+ and Hg 2+ . SHARMA et al (2001) reported inhibition of Pseudomonas sp. AG-8 lipase by Hg 2+ .…”

Section: Resultsmentioning

confidence: 99%

“…The findings are in agreement et al 1991) and Aspergillus oryzae (TOIDA et al 1998). ABBAS et al (2002) and SHARMA et al (2001 reported inhibitory effects of Triton X-100 and SDS on lipase from Mucor sp. and Pseudomonas sp.…”

Section: Resultsmentioning

confidence: 99%

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Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Sekhon

Dahiya

Tiwari

et al. 2005

J. Basic Microbiol.

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An extracellular lipase isolated from Bacillus megaterium AKG-1 had an optimum activity at 55 degrees C/pH 7.0. It retained 100% activity at 50 degrees C for 30 min with a half life of 30 min at 70 degrees C. A 20-70% increase in lipase activity was observed in presence of acetone (20% v/v), DMSO (20% v/v) and isopropanol (10% v/v). The enzyme activity was 92, 98 and 107% after 24 h, on treatment with 10% (v/v) acetone, benzene and isopropanol respectively. Deoxycholic acid, sodium deoxycholate, lithocholic acid, rhamnolipid, Brij 52 and cholic acid stimulated the lipase activity by 76, 36, 24, 24, 23.6 and 13%, respectively. Addition of reducing agents like sodium sulphite, sodium metabisulphite and L-cysteine-HCl, at 10 mM concentration stimulated lipase activity by 127, 146 and 150% respectively. The lipase appeared to show enantioselectivity in hydrolyzing racemic 3-acetoxy-beta-lactam as it hydrolyzed only the (+) enantiomer.

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

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Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Sekhon

Dahiya

Tiwari

et al. 2005

J. Basic Microbiol.

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“…This property is similar to the extracellular lipase from a Pseudomonas sp. AG-8, it shows 4.5-fold enhanced lipase activity with 20% (v/v) acetone (Sharma et al 2001). For stepwise precipitation the method involved using acetone at different saturations (Table 1).…”

Section: Resultsmentioning

confidence: 99%

Purification of lipase from Cunninghamella verticillata by stepwise precipitation and optimized conditions for crystallization

Kumarevel

Gopinath

Amanda

et al. 2005

World J Microbiol Biotechnol

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Lipase from the oil-mill waste isolate Cunninghamella verticillata was purified by stepwise precipitation using acetone, as a sequel to our earlier conventional column chromatographic method [Gopinath et al. (2002) World Journal of Microbiology and Biotechnology 18, 449-458]. The yield of purified lipase was approx. 4-fold higher than by the previous method and the purified lipase was obtained with 70-80% acetone saturations. The enzyme was resolved as a single band with homogeneity both by native and by SDS-PAGE. The optimum condition for the lipase to crystallize was 5 lg of enzyme in 0.05 M sodium phosphate buffer (pH 6.5) with 5 mM FeCl 2 and 10% 2-methyl 2,4-pentanediol (MPD).

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“…Microbial lipase production is usually carried out using submerged fermentation technique [9], however solid state fermentation methods have also been found to be beneficial [10]. Lipid carbon sources have been found to be generally important for obtaining a high lipolytic enzyme yield although a few researchers have obtained substantial lipase yields without using fats or oils [4].…”

Section: Introductionmentioning

confidence: 99%

Production and Partial Characterization of Lipase from Pseudomonas putida

Fatima¹,

Khan²

2015

Ferment Technol

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The production of lipase from Pseudomonas putida 922 was optimized by modifying various physical parameters such as carbon source, nitrogen source, pH, salt concentration and biochemical parameters of the production medium such as temperature and incubation time of the growth medium. Oil cakes were also used as carbon source to check for an increased production of the enzyme. The bacterium was found to have a maximal growth at pH 10 with the enzyme production being highest (24 U/ml) after 48 hours at 30°C and pH 10. The optimum composition of the medium was mustard oil cake as carbon source, yeast extract or peptone as nitrogen source and 1% sodium chloride concentration. Partial characterization of the enzyme was carried out where the optimum working pH and temperature was found to be 10 and 40ºC, respectively. Enzyme stability was found to lie in the pH and temperature ranges of 5-11 and 30-40ºC, respectively. Partial purification of the enzyme was carried out at 80% ammonium sulphate saturation. Molecular mass of lipase was determined by SDS PAGE and found to be 45 kDa.

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Properties of a thermostable and solvent stable extracellular lipase from aPseudomonas sp. AG-8

Cited by 29 publications

References 14 publications

Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Purification of lipase from Cunninghamella verticillata by stepwise precipitation and optimized conditions for crystallization

Production and Partial Characterization of Lipase from Pseudomonas putida

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