Influence of multiple bioprocess parameters on production of lipase from Pseudomonas sp. BWS-5

Sooch, Balwinder Singh; Kauldhar, Baljinder Singh

doi:10.1590/s1516-89132013000500002

Cited by 31 publications

(18 citation statements)

References 20 publications

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“…This is due to the presence of oleic acid in large quantities in olive oil (78%) because lipases are of the inductive type with a preference for monounsaturated long chain fatty acids. These results are consistent with several studies on microbial lipases showing a high production of lipase in the presence of olive oil among several oils tested (Feitosa et al, 2010;Sooch and Kauldhar, 2013;Iqbal and Rehman, 2015;Quian and Chun-Yun, 2009;Nwachukwu et al, 2017;Vishnupriya et al, 2010;Esakkiraj et al, 2010;Dandavate et al, 2009). An important lipolytic activity is also observed with 2% olive oil in other bacterial species, like Pseudomonas aeruginosa KM110 and Bacillus sp ZR-5 (Mobarak-Qamsari et al, 2011;Soleymani et al, 2017).…”

Section: Intracellular Lipolytic and Esterase Activitiessupporting

confidence: 92%

Lipase and esterase activities of lactic acid bacteria isolated from different biotopes

Dellali¹,

Karam²,

Karam³

2020

Afr. J. Biotechnol.

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The lipolytic and esterase activities of fifteen strains of lactic acid bacteria isolated from different biotopes of Algeria and Mauritania were tested on MRS medium supplemented with lipidic substrates. Five of them showed maximum activity in the presence of tributyrin; the activity is therefore a tributyrin esterase. These strains were identified by MALDI-TOF in Enterococcus faecium and Enterococcus durans. The study of growth kinetics as a function of time shows a start of fatty acid production during the exponential phase to reach its maximum in the stationary phase. A better esterase activity is observed at between pH 6 and 9 and at an optimal temperature of 30 to 40°C for the five strains. The influence of metal and additive ions on the esterase activity varies between bacteria but generally, total inhibition was observed in all strains tested in the presence of SDS, NaN 3 , CuCl 2 , EDTA, AgNO 3 and HgCl 2 .

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Section: Intracellular Lipolytic and Esterase Activitiessupporting

confidence: 92%

Lipase and esterase activities of lactic acid bacteria isolated from different biotopes

Dellali¹,

Karam²,

Karam³

2020

Afr. J. Biotechnol.

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“…Enzyme activity had a significant elevation under agitation when compared with the stationary state. Enzyme production increased when the agitation rate increased up to 150 rpm, and, subsequently, a reduction in activity was reported (Sooch and Kauldhar, 2013). The decrease in enzyme activity at elevated agitation rates might be attributed to the depletion in the nutrient level and oxygen in the medium and the shared stress on bacterial cells in addition to enzyme structure (Calderbank and Moo-Young, 1959).…”

Section: Resultsmentioning

confidence: 99%

Production of Cold-Active Lipase by Free and Immobilized Marine Bacillus cereus HSS: Application in Wastewater Treatment

2018

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Lipases are enzymes that have the potential to hydrolyze triacylglycerol to free fatty acids and glycerol and have various applications. The aim of the present study was to isolate and screen marine bacteria for lipase production, optimize the production, and treat wastewater. A total of 20 marine bacterial isolates were obtained from the Mediterranean Sea and were screened for lipase production. All isolates were found to have lipolytic ability. The differences between the isolates were studied using RAPD-PCR. The most promising lipase producer (isolate 3) that exhibited the highest lipolytic hydrolysis (20 mm) was identified as Bacillus cereus HSS using 16S rDNA analysis and had the accession number MF581790. Optimization of lipase production was carried out using the Plackett–Burman experimental design with cotton seed oil as the inducer under shaking conditions at 10°C. The most significant factors that affected lipase production were FeSO4, KCl, and oil concentrations. By using the optimized culture conditions, the lipase activity increased by 1.8-fold compared with basal conditions. Immobilization by adsorption of cells on sponge and recycling raised lipase activity by 2.8-fold compared with free cells. The repeated reuse of the immobilized B. cereus HSS maintained reasonable lipase activity. A trial for the economic treatment of oily wastewater was carried out. Removal efficiencies of biological oxygen demand, total suspended solids, and oil and grease were 87.63, 90, and 94.7%, respectively, which is promising for future applications.

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“…Increase in temperature increases the rates of enzymatic reactions in cells till it reaches the optimum. Beyond the optimum temperature, the enzyme is inactivated due to denaturation of the protein causing slow metabolism of the cells and affect the cell growth and productivity (Sooch and Kauldhar, 2013).…”

Section: Effect Of Temperature On Lipase Activitymentioning

confidence: 99%

“…Then, 60 min was the optimum time of incubation for enzyme activity and gave 30 U/ml. This decline in enzyme activity could be due to the denaturation and structure modification in the enzyme or to catabolite repression of enzyme (Sooch and Kauldhar, 2013).…”

Section: Effect Of Incubation Period On Lipase Activitymentioning

confidence: 99%

“…Also, the maximum activity of the lipase from Pseudomonas spp. BWS-5 (223.5 IU/ml) was obtained at pH 6.5 and temperature 37°C by Sooch and Kauldhar (2013) and thereafter, it decline. Also P. fluorescens SIK W1 has an acidic optimum pH 4.8 (Qamsari et al, 2011), while P. fluorescens 2D (Makhzoum et al, 1996) and P. cepacia (Svendsen et al, 1995) have pH optima of 8.5 and 9.0, respectively.…”

Section: Effect Of Ph On Lipase Activitymentioning

confidence: 99%

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Characterization and optimization of lipase activity produced by Pseudomonas monteilli 2403-KY120354 isolated from ground beef

Rasmey¹,

Aboseidah²,

Gaber³

et al. 2017

Afr. J. Biotechnol.

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A total of 56 Gram negative bacterial isolates were recovered from twenty ground beef samples and were screened for their potentiality to produce lipase. Forty four bacterial isolates were recorded as positive producers for lipase on tween as carbon source in solid medium. Also, the highly producer isolates were screened for lipase activity in submerged culture using olive oil as carbon and the most active isolate was 2043 which gave an activity of 20.0 ± 0.29 U/ml. The bacterial isolate 2403 was identified phenotypically according to Bergey's Manual and genotypically using 16S rRNA genes analysis as Pseudomonas monteilli. Effect of some different factors on lipase activity were studied and the maximum lipase activity was achieved at reaction medium of pH 6 and incubated at 40°C for 60 min. Also, addition of Ba 2+ in the reaction medium enhanced the lipase activity, while the other tested metals reduced the enzyme activity.

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Influence of multiple bioprocess parameters on production of lipase from Pseudomonas sp. BWS-5

Abstract: The aim of the present work was to study the influence of multiple bioprocess parameters for the maximum production of lipase from Pseudomonas sp. (1 %, w/v), peptone (3 %, w/v) and KCl (0.05 %, w/v)

Cited by 31 publications

References 20 publications

Lipase and esterase activities of lactic acid bacteria isolated from different biotopes

Lipase and esterase activities of lactic acid bacteria isolated from different biotopes

Production of Cold-Active Lipase by Free and Immobilized Marine Bacillus cereus HSS: Application in Wastewater Treatment

Characterization and optimization of lipase activity produced by Pseudomonas monteilli 2403-KY120354 isolated from ground beef

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