Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/1643
Title: Studies on crystallization and cross-linking of lipase for biocatalysis
Authors: Akhila Rajan
Emilia Abraham, T
Keywords: Ibuprofen
Thermal stability
CLEC lipase
Organic Solvent
Issue Date: 2008
Publisher: Springer
Citation: Bioprocess and Biosystems Engineering 31(2):87-94;Feb 2008
Abstract: The development of robust biocatalysts with increased stability and activity is a major challenge to industry. A major breakthrough in this field was the development of cross-linked enzyme crystals with high specificity and stability. A method is described to produce micro crystals of CLEC lipase, which is thermostable and solvent stable. Lipase from Burkholderia cepacia was crystallized using ammonium sulfate and cross-linked with glutaraldehyde to produce catalytically active enzyme. The maximum yield of CLEC was obtained with 70% ammonium sulfate and cross-linked with 5% (v/v) glutaraldehyde. SEM studies showed small hexagonal-shaped crystals of 2-5 mu m size. CLEC lipase had improved thermal and reuse stability. It is versatile, having good activity in both polar and nonpolar organic solvents. CLEC lipase was coated using beta cyclodextrin for improving the storage and reuse stability. CLEC was successfully used for esterification of Ibuprofen and synthesis of ethyl butyrate.
ISSN: 1615-7591
Appears in Collections:2008

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