“…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. The similar finding to our results, Benattouche and Abbouni (2012) showed that P. aeruginosa was able to grow in the pH range from 6 to 8 and reached the maximum lipase activity of 38.5 U/ml at pH 7. and Ba 2+ ) were examined for their effect on lipase activity. As represented by Figure 6, it was revealed that Zn 2+ lowered lipase activity to 20% and Cd 2+ dramatically lowered lipase activity to 12%, while the activity nearly remained constant (26 to 28%) using Cu 2+ and Mn 2+ and increased 28% using Ba 2+ .…”
Section: Effect Of Ph On Lipase Activitysupporting
confidence: 81%
“…The obtained results revealed that a total of 14 isolates were moderate (18 to 23 mm), while five isolates were investigated as high (24 to 32 mm) producers for lipase activity and the remaining positive tested isolates were recorded as low (<18 mm) lipase producers. Evaluation of the lipase-producing efficiency, based on the clear zone around colony, indicated that all Pseudomonas isolates produced lipase enzyme (Benattouche and Abbouni, 2012 3070 were selected for secondary screening to determine the most active isolate for lipase production in broth medium using olive oil as a substrate.…”
Section: Isolation and Detection Of Lipolytic Bacteriamentioning
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.
“…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. The similar finding to our results, Benattouche and Abbouni (2012) showed that P. aeruginosa was able to grow in the pH range from 6 to 8 and reached the maximum lipase activity of 38.5 U/ml at pH 7. and Ba 2+ ) were examined for their effect on lipase activity. As represented by Figure 6, it was revealed that Zn 2+ lowered lipase activity to 20% and Cd 2+ dramatically lowered lipase activity to 12%, while the activity nearly remained constant (26 to 28%) using Cu 2+ and Mn 2+ and increased 28% using Ba 2+ .…”
Section: Effect Of Ph On Lipase Activitysupporting
confidence: 81%
“…The obtained results revealed that a total of 14 isolates were moderate (18 to 23 mm), while five isolates were investigated as high (24 to 32 mm) producers for lipase activity and the remaining positive tested isolates were recorded as low (<18 mm) lipase producers. Evaluation of the lipase-producing efficiency, based on the clear zone around colony, indicated that all Pseudomonas isolates produced lipase enzyme (Benattouche and Abbouni, 2012 3070 were selected for secondary screening to determine the most active isolate for lipase production in broth medium using olive oil as a substrate.…”
Section: Isolation and Detection Of Lipolytic Bacteriamentioning
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.
“…The standard liquid medium for measurement the lipase activity according 16 use for culturing lipase producing bacteria. the broth media were inoculated of 5% overnight culture media of all the lipase producing isolates was prepared according to 17 , the medium consist of (g/L): yeast extract, 2.5; pepton, 5.5; NaCl, 10 and 1% olive oil, autoclaving at 121°C for 15 min.…”
Bacterial lipases are the most important collection of biocatalysts used for a variety of biotechnological applications. In the current study the morphological, biochemical and Molecular characteristics to the extracellular lipase producing bacteria were identified. The bacterial isolates were selected as lipase producing bacteria using Rhodamine-B agar plate. the production of Lipase from the organism were determined with varying incubation temperature (20 to 50°C) and range of incubation time (16-120) hrs. 16 bacterial isolates were identified as Staphylococcus hemolyticus strain SHKS1 with Genbank acc. MK977614.1. By comparing the observed DNA sequences of these local samples with the retrieved DNA sequences (GenBank acc. MG595372.1) as showed high lipase activity according to experimental conditions about 140 U/ml. The current study showed that enzymatic activity of crude lipase extract was maximum in 72 hrs incubation period and 37°C.
“…The production of lipase in the present study was carried out by using the selected isolate Pseudomonas aeruginosa and the optimum conditions for lipase production according of [15], the basal salt medium for lipase production was prepared according to [16]. The medium was inoculated with 6 ml of the overnight culture was prepared according to [17].…”
Section: Lipase Producing Isolatementioning
confidence: 99%
“…The lipase crude was extracted according to [16]. The supernatant was collected and sterilized using 0.22µm Millipore filter paper.…”
Section: Lipase Crude Extraction Produced By P Aeruginosa Isolatementioning
The present study aimed to Purification and characterization of lipase produced by the isolate Pseudomonas aeruginosa. The results showed that crude lipase was purified by using the precipitation step of several concentrations ratios of cold acetone. The concentration ratio 4:1 gave the best specific activity 6 U/mg of protein. The subsequent purification step using gel filtration was showed that specific activity reached to 40.5U/mg of protein. The gel electrophoresis (SDS-PAGE) of lipase purity were determined. the result showed there is an appearance of a single protein band predominant in all purification steps, While The molecular weight of purified lipase was 68KDa
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