Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus

Samaei-Nouroozi, Amene; Rezaei, Shahla; Khoshnevis, Nika; Doosti, Mahmood; Hajihoseini, R; Khoshayand, Mohammad Reza; Faramarzi, Mohammad Ali

doi:10.1007/s00792-015-0769-7

Cited by 46 publications

(20 citation statements)

References 42 publications

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“…of halophilic lipases is not compromised even in presence of very high concentration of organic solvents, they are very promising candidates for carrying out lipase-catalyzed organic biotransformation [1][2][3].…”

Section: Insights In Enzyme Researchmentioning

confidence: 99%

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Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Hemamalini¹,

Sk²

2018

Insights Enzyme Res

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Background: Marinobacter is a halophilic bacterial genus and a bio-geochemically important group in sea water, is generally associated with the bioremediation of hydrocarbon-rich effluents released into the salt-rich environment by various anthropogenic activities. It is a well-known lipase producer-the NCBI Protein database shows nearly 520 Marinobacter lipases. In this context, its lipase and esterase are considered important. However, their enzymatic properties in purified form have been scantily studied. Since hydrocarbons are acted upon on solvent water interface, the stability and catalytic behavior of Marinobacter lipase in non-aqueous media needs to be more specifically investigated.Aim: Marinobacter sp. EMB5 was isolated from Kozhikode, Kerala, India. It was found to be potent lipase producer. The aim of the present work was to obtain a purified preparation and undertake its detailed characterization with respect to above aspects. Work:The crude Marinobacter sp. lipase was purified by Sephacryl S200 gel filtration chromatography. The lipase eluted as a single activity peak in void volume and had a very high molecular mass. Aggregation has not been reported in case of Marinobacter lipase, so far, although it is known in other lipases. The aggregated lipase was mixed with 2-propanol (70%, v/v) and disaggregated lipase was obtained as a single activity peak in Sephacryl S200 gel filtration chromatography corresponding to 82 kDa molecular mass. This monomeric species was less active than aggregated purified preparation. Hence, further characterization and studies were carried out on purified active aggregate lipase. It was stable in a wide range of organic solvents at high concentration up to 24 h. The organic solvent stability was further investigated by Far UV CD spectroscopy and fluorescence spectroscopy. Conclusion:Due to the fact that Marinobacter sp. EMB5 lipase remained stable in organic solvents for prolonged incubation periods, it has potential to be used in industrial organic synthesis.

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Section: Insights In Enzyme Researchmentioning

confidence: 99%

“…Polar solvents are known to strip off essential water of activity from active site universally causing loss in activity, so was in the present case. Among the halophilic lipases, solvent stability has been reported from Haloarcula, Idiomarina, Alkalibacillus salilacus [2,3,5].…”

Section: Characterization Of Purified Lipasementioning

confidence: 99%

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Hemamalini¹,

Sk²

2018

Insights Enzyme Res

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“…Carbon sources have often been considered as an important parameter for the expression of lipase activity due to the inducible nature of lipases. Maltose has been reported as an enhancer of lipase secretion in some organisms [21]. Although, some authors [22][23][24] have recorded the enhanced lipase production when glucose and olive oil were used in combination as carbon sources, contrarily, a low lipase yield was recorded in this case.…”

Section: Discussionmentioning

confidence: 85%

“…The result shown in this research aligns with the work of Pérez et al , where 1–2% (v/v) olive oil was used for detecting the hydrolytic potential of a moderate halophilic bacterium, M. lipolyticus SM19. Higher levels of lipase activity have been shown from different microorganisms with the olive oil as a lipidic carbon source .…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, the repressive influence of glucose on lipase secretion may be related to catabolite regulation mechanism in bacteria that keeps sugar utilization to a certain level according to the organism's metabolic capacity [26]. Lipidic carbon sources, such as natural oils induce lipase secretion, whereas carbon sources that are conveniently metabolized and utilized by bacteria show an inhibitory effect [21]. The repressive influence of glucose on lipase biosynthesis was documented by Ramos-Sánchez et al [27] and Kumar and Kanwar [28].…”

Section: Discussionmentioning

confidence: 99%

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Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

et al. 2018

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An approach was made to enhance the halophilic lipase secretion by a newly isolated moderate halophilic Marinobacter litoralis SW‐45, through the statistical optimization of Plackett‐Burman (PB) experimental design and the Face Centered Central Composite Design (FCCCD). Initially, PB statistical design was used to screen the medium components and process parameters, while the One‐factor‐at‐a‐time technique was availed to find the optimum level of significant parameters. It was found that MgSO4 · 7H2O, NaCl, agitation speed, FeSO4 · 7H2O, yeast extract and KCl positively influence the halophilic lipase production, whereas temperature, carbon source (maltose), inducer (olive oil), inoculum size, and casein‐peptone had a negative effect on enzyme production. The optimum level of halophilic lipase production was obtained at 3.0 g L−1 maltose, 1% (v/v) olive oil, 30 °C growth temperature and 4% inoculum volume (v/v). Further optimization by FCCCD was revealed 1.7 folds improvement in the halophilic lipase production from 0.603 U ml−1 to 1.0307 U ml−1. Functional and biochemical characterizations displayed that the lipase was significantly active and stable in the pH ranges of 7.0–9.5, temperature (30–50 °C), and NaCl concentration (0–21%). The lipase was maximally active at pH 8.0, 12% (w/v) NaCl, and 50 °C temperature. Besides, M. litoralis SW‐45 lipase was found to possess the promising industrial potential to be utilized as a biocatalyst for the esterification.

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Biochemical characterization of an organic solvent‐tolerant glycosyltransferase from Bacillus licheniformis PI15 with potential application for raspberry ketone glycoside production

Fan

et al. 2019

Biotech and App Biochem

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Raspberry ketone is a primary aroma component of the red raspberry. The glycosylation of this compound is a potential approach used to improve its pharmaceutical properties. In this work, raspberry ketone glycosides are produced in bacteria for the first time. Bacillus licheniformis PI15, an organic solvent‐tolerant glycosyltransferase‐producing strain, was isolated from chemically polluted soil. The cloning and heterologous expression of a glycosyltransferase, which was designated PI‐GT1, in Escherichia coli BL21 resulted in the expression of an active and soluble protein that accounted for 15% of the total cell protein content. Purified PI‐GT1 was highly active and stable over a broad pH range (6.0–10.0) and showed excellent pH stability. PI‐GT1 maintained almost 60% of its maximal activity after 3 H of incubation at 20–40 °C and demonstrated optimal activity at 30 °C. Additionally, PI‐GT1 displayed high stability and activity in the presence of hydrophilic solvents with log P ≤ −0.2 and retained more than 80% of its activity after 3 H of treatment. Supplementation with 10% DMSO markedly improved the glycosylation of raspberry ketone, resulting in a value 26 times higher than that in aqueous solution. The organic solvent‐tolerant PI‐GT1 may have potential uses in industrial chemical and pharmaceutical synthesis applications.

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Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus

Cited by 46 publications

References 42 publications

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

Biochemical characterization of an organic solvent‐tolerant glycosyltransferase from Bacillus licheniformis PI15 with potential application for raspberry ketone glycoside production

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