Document Detail


Immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate: solvent effect.
MedLine Citation:
PMID:  18255281     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate was studied in twelve different solvents in order to deduce the solvent effect through an attempt to correlate the highest yield with such solvent properties as hydrophobicity (log P), dielectric constant (epsilon), and Hildebrand solubility parameter (delta). The results showed that the conversion of glycerol trioleate and yield of oleic acid methyl ester were quite dependent on the solvent. The catalyst lipase in various solvents also needed different optimum amount of water to keep its maximum activity, and generally this lipase in more hydrophobic solvents required more water. The correlation between the highest yield and log P value was found to be reasonable except deviation of data points of certain solvents, while no obvious correlation existed between the other two parameters, dielectric constant (epsilon) and Hildebrand solubility parameter (delta), and the enzyme activity. The study revealed that more hydrophobic solvents such as n-hexane or cyclohexane were more suitable solvents for Candida sp. 99-125 catalyzed transesterification of glycerol trioleate to oleic acid methyl ester.
Authors:
Jike Lu; Kaili Nie; Fang Wang; Tianwei Tan
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-02-05
Journal Detail:
Title:  Bioresource technology     Volume:  99     ISSN:  0960-8524     ISO Abbreviation:  Bioresour. Technol.     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-05-26     Completed Date:  2008-08-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9889523     Medline TA:  Bioresour Technol     Country:  England    
Other Details:
Languages:  eng     Pagination:  6070-4     Citation Subset:  IM    
Affiliation:
Beijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China. ljk002004@163.com
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Candida / enzymology*
Catalysis
Enzymes, Immobilized / metabolism*
Lipase / metabolism*
Methane / metabolism*
Solvents
Triolein / metabolism*
Chemical
Reg. No./Substance:
0/Enzymes, Immobilized; 0/Solvents; 122-32-7/Triolein; 74-82-8/Methane; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Pancreaticoduodenectomy for presumed pancreatic cancer.
Next Document:  Effect of substrate concentration on dry mesophilic anaerobic digestion of organic fraction of munic...