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