Document Detail


Improved enzymatic activity of Thermomyces lanuginosus lipase immobilized in a hydrophobic particulate mesoporous carrier.
MedLine Citation:
PMID:  20022021     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lipase from Thermomyces lanuginosus has been immobilized within particulate mesoporous silica carriers, with either hydrophilic or hydrophobic supporting surfaces, produced by the newly developed emulsion and solvent evaporation (ESE) method. The Michaelis-Menten model was used to calculate the parameters related to the enzymatic activity of lipase i.e. the turnover number, k(cat), and the specific activity. The specific activity was improved by immobilization of lipase onto the hydrophobic support, compared to lipase immobilized onto the hydrophilic support and lipase free in solution. The enhanced enzymatic activity of lipase onto a hydrophobic support was attributed to interfacial activation of the Thermomyces lanuginosus lipase when it is attached to a hydrophobic surface and a reduced denaturation. Confocal scanning laser microscopy (CLSM) studies, of fluorescently tagged lipase, showed that leakage of the lipase from the mesoporous particles was limited to an initial period of only a few hours. Both the rate and the amount of lipase leached were reduced when the lipase was immobilized onto the hydrophobic support.
Authors:
Malin H S?rensen; Jovice B S Ng; Lennart Bergstr?m; Peter C A Alberius
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-11-10
Journal Detail:
Title:  Journal of colloid and interface science     Volume:  343     ISSN:  1095-7103     ISO Abbreviation:  J Colloid Interface Sci     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-01-28     Completed Date:  2010-04-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0043125     Medline TA:  J Colloid Interface Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  359-65     Citation Subset:  IM    
Copyright Information:
2009 Elsevier Inc. All rights reserved.
Affiliation:
YKI, Institute for Surface Chemistry, Box 5607, SE-114 86 Stockholm, Sweden. Malin.sorensen@yki.se
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MeSH Terms
Descriptor/Qualifier:
Ascomycota / enzymology*
Enzymes, Immobilized / chemistry,  metabolism*
Hydrophobicity
Lipase / chemistry,  metabolism*
Porosity
Chemical
Reg. No./Substance:
0/Enzymes, Immobilized; EC 3.1.1.3/Lipase

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