An extra-cellular alkaline metallolipase from Bacillus licheniformisMTCC 6824: Purification and biochemical characterization

Chakraborty, Kajal; Raj, Rashmi

doi:10.1016/j.foodchem.2008.01.026

Cited by 58 publications

(53 citation statements)

References 18 publications

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“…The accumulation of more than two mutations had a dramatic impact on Geobacillus thermodenitrificans EstGtA2 lipase activity at high temperatures, suggesting an important role of conserved salt bridge-forming residues in thermostability (Charbonneau and Beauregard, 2013). Alkaline lipases are widely produced by the members of Bacillus genera, including B. licheniformis (Chakraborty and Raj 2008). Organic solvent tolerance is yet another useful trait, desirable for catalyzing synthetic reactions in nearly anhydrous conditions and has been observed in B. sphearicus (Tamilarasan and Kumar 2012).…”

Section: Sources Of Microbial Lipasesmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

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Section: Sources Of Microbial Lipasesmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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“…A particular interest relies on lipases capacity of catalysing such reactions and, consequently, the synthesis of fine compounds used for manufacturing products of high aggregate value, such as the engineering of structured lipids for the biotransformation of oils and fats [3][4][5][6]. Each application requires unique properties with respect to specificity, stability, optimal temperature, and pH-dependence [7]. In order to use lipases for hydrolysis, esterification, or other applications, it is essential to produce the purified enzyme at high concentrations and to determine its biochemical properties.…”

Section: Introductionmentioning

confidence: 99%

Expression, purification of a novel alkaline Staphylococcus xylosus lipase acting at high temperature

Bouaziz¹,

Horchani²,

Salem³

et al. 2011

Biochemical Engineering Journal

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a b s t r a c tA new Staphylococcus xylosus strain was isolated. The extracellular lipase of S. xylosus (wt-SXL2) was purified to homogeneity from the culture medium. The specific activity of the purified enzyme, measured at pH 8.5 and 55• C using tributyrin or olive oil emulsion, reached, respectively, 6300 U/mg or 2850 U/mg. The sequenced 18 N-terminal amino acid showed a high degree of identity with known staphylococcal lipase sequences.The gene encoding the mature lipase was cloned and sequenced. The deduced amino acid sequence showed a significant similarity with various staphylococcal lipases. The highest overall identity (98.74%) was found with S. xylosus lipase (SXL1). The mature part of the lipase was expressed in Escherichia coli. The recombinant lipase was purified by affinity chromatography. The specific activity of the recombinant lipase was 4100 or 1500 U/mg using tributyrin or olive oil emulsion as substrate, respectively, at pH 8.5 and 55• C. The wild type and recombinant lipases presented a quite interesting thermal stability, after an incubation of 60 min at 55• C and they are found to be highly stable at a pH ranging from 4 to 11. Due to its stability at high temperature and in organic solvent, the wt-SXL2 was used as biocatalyst to synthesise a high added value molecules.

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“…Also, lipases do not require cofactors to catalyse hydrolytic reactions and remain active in the presence of organic solvents 5 . Bacterial lipases are produced by both submerged and solid-state fermentation 6,7 . Lipase production requires carbon and nitrogen sources as required by any fermentation process.…”

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confidence: 99%