Purification and Characterization of a Thermostable Lipase fromGeobacillus thermodenitrificansIBRL-nra

Balan, Andrea; Demirtaş, İbrahim; Rahim, Rashidah Abdul; Rashid, Fatimah Azzahra Ahmad

doi:10.1155/2012/987523

Cited by 57 publications

(37 citation statements)

References 34 publications

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“…Likewise, the activity was measured at different pH values and found to be maximal at pH 9.0-10.0. These conditions match those determined for other thermophilic lipases and phospholipases [Balan et al, 2012;Tirawongsaroj et al, 2008].…”

Section: Discussionsupporting

confidence: 82%

Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities

et al. 2018

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Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55–80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes.

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Section: Discussionsupporting

confidence: 82%

Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities

et al. 2018

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“…4D) stable in an alkaline environment [20][21][22]. Thermostable lipase from Geobacillus thermodenitrificans IBRL-nra retains more than 80% of its original activity for 24 H at pH 6.5-7.5 [23]. Table 1).…”

Section: Effects Of Ph On Lipase Activity and Stabilitymentioning

confidence: 99%

Screening and characterization of a thermostable lipase from marineStreptomycessp. strain W007

Yuan

Lan

Xin

et al. 2015

Biotech and App Biochem

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A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X-33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well-characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0-9.0. It was stable and retained about 90% of initial activity in the presence of Cu(2+) , Ca(2+) , Ni(2+) , and Mg(2+) , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application.

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“…The speed of 110 rpm favoured mycelial growth (30.0 mg dry weight) of the isolate but the production was favored by 120 rpm (38.7 U/ml).In the previous study, the agitation speed of m125 rpm favored lipase production 32 . Agitation speed of 200 rpm favored the lipase production in the previous study 15 .…”

Section: Agitationmentioning

confidence: 65%

“…The enzyme lipase is produced by a variety of microorganisms including Fusarium oxysporum 11 , Pseudomonas aeroginosa 12 , Aspergillusoryzae CJLU-31 13 , Bacillus pumilis RK 31 14 , Geobacillus thermodentrificans IBRL-nra 15 , Streptomyces griseus 16 and Streptomyces aurofaciens 17 .…”

Section: Introductionmentioning

confidence: 99%

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2013

IJPSR

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Partial purification and bioremediation of waste water by lipase from the marine actinomycete Streptomyces variabilis NGP 3 (Accession no: (JX843530)) were carried out. The optimum incubation period, pH, temperature and agitation speed for enzyme production were fifth day (61.2 U/ml), 9.0 -9.5 (105 U/ml), 35ºC (39.4 U/ml) and 120 rpm (38.7 U/ml) respectively. Lactose (2.0 g/l) and peptone (0.6 and 0.8 g/l) proved to the best carbon and nitrogen sources respectively for lipase production. The partially purified lipase showed a specific activity of 1440.97 U/mg protein, 7.63 fold pure and yielded 3.19 per cent of protein. The enzyme activity was maximum at the pH and temperatures were 8.5 and 45ºC respectively. The molecular weight of the first and second isoenzymes was found to be 55.0 and 56.0 KDa respectively. Bioremediation of automobile effluent and slaughter house waste water were carried out by the isolated actinomycetes isolate S. variabilis NGP 3. The chemical oxygen demand (COD), total organic chloride (TOC) and fat/oil content of the effluent were analyzed. The COD and fat/oil degradation rate were increased by the simultaneous reduction of TOC in the treated effluent.

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Purification and Characterization of a Thermostable Lipase fromGeobacillus thermodenitrificansIBRL-nra

Cited by 57 publications

References 34 publications

Characterization of a Novel Thermostable Enzyme from <b><i>Thermus</i></b> sp. 2.9 with Phospholipase and Acyltransferase Activities

Characterization of a Novel Thermostable Enzyme from <b><i>Thermus</i></b> sp. 2.9 with Phospholipase and Acyltransferase Activities

Screening and characterization of a thermostable lipase from marineStreptomycessp. strain W007

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