Publication | Open Access
Identification of potential fungal strain(s) for the production of inducible, extracellular and alkalophilic lipase
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Citations
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References
2007
Year
Alkalophilic LipaseEngineeringFungal Cell BiologyEnzymatic ModificationBiosynthesisEnzymologyPlant EnzymesLipid SubstratesPotential Fungal StrainBiochemistryBiocatalysisLipid ResourceChain Fatty AcidsFungal PhysiologyFungal Cell FactoryBiomolecular EngineeringNatural SciencesEnzyme CatalysisBiotechnologyEnzyme SpecificityMicrobiology
During the last twenty years, the industrial use of enzymes has rapidly increased. Lipases have gained importance to a certain extent over proteases and amyla-ses especially in the area of organic synthesis. Lipases are a class of water insoluble enzymes that catalyse the hydrolysis of ester bonds in lipid substrates, such as triacylglycerols (TAGs) releasing long chain fatty acids. Apart from hydrolysis, they bring about a wide range of conversion reactions that include interesterifications, alcoholysis and aminolysis. The unique characteristics of lipases include substrate specificity, stereospecificity, regiospecificity, and the ability to catalyse a heteroge-neous reaction at the interface of water soluble and water insoluble systems (Macrae and Hammond, 1985). Lipases are produced by plants, animals, bacteria and molds. Plant enzymes are not used commercially while animal, bacterial and mold enzymes are used extensive- B
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