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Advantages of the Immobilization of Lipase on Porous Supports Over Free Enzyme

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Abstract:

In this work, we have compared the stability and activity of immobilized lipase and free enzyme of same specific activity. The immobilization was carried out on (3Å x 1.5 mm) molecular sieve (a porous support) derivatized with glutaraldehyde as the functional group. Immobilization of the enzyme allowed the maintenance of 85% of the enzyme activity even after 8th cycle. In fact, only 12% of the enzyme activity was lost whereas the soluble enzyme lost 90% of its initial activity when incubated at 55°C for 2 hrs. Additionally, the enzyme was stable between pH 7.5-9.0 unlike free enzyme. Kinetic parameters Km and Vmax for free and molecular sieve-immobilized lipase were found to be 0.3 mM and 1 μmole/min/ml, 3.7 mM and 8 μmole/min/ml, respectively. Moreover, the immobilized enzyme, on the porous support, cannot be denatured with detergents, and, therefore, it maintained the stability achieved by means of the multipoint covalent attachment on the molecular sieve support.





Keywords: BTS-1 lipase; Bacillus coagulans; Bacillus coagulans BTS-3; Candida rugosa; Catalytic; DEAE-Sepharose column chromatography; Detergents; Free Enzyme; Hydrolytic; Kinetics; Km; Lineweaver-Burke curve; Lipase assay; Porous; SDS; Vmax; absorbance; coagulans; colorimetric method; glutaraldehyde; immobilization; lipase; molecular; molecular sieve; pH

Document Type: Research Article

Publication date: November 1, 2010

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2010/00000017/00000011/art00013
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