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Superior activities of lipase immobilized on pure and hydrophobic clay supports: Characterization and catalytic activity studies.

Authors :
Reshmi, R.
Sugunan, S.
Source :
Journal of Molecular Catalysis B: Enzymatic. Dec2013, Vol. 97, p36-44. 9p.
Publication Year :
2013

Abstract

Highlights: [•] Lipase was immobilized onto montmorillonite via adsorption and covalent binding. [•] The immobilized enzymes displayed enhanced catalytic efficiency and storage stability. [•] The activity of the free lipase in heptane was 0.51% of that in the aqueous medium. [•] The organomodified nanoclays would be suitable for industrial biotransformations. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
13811177
Volume :
97
Database :
Academic Search Index
Journal :
Journal of Molecular Catalysis B: Enzymatic
Publication Type :
Academic Journal
Accession number :
91629349
Full Text :
https://doi.org/10.1016/j.molcatb.2013.04.003