Document Detail

Fatty acid selectivity of lipases during acidolysis reaction between triolein and saturated fatty acids varying from caproic to behenic acids.
MedLine Citation:
PMID:  19645505     Owner:  NLM     Status:  MEDLINE    
The chain length selectivity of three immobilized lipases, namely, Lipozyme TL IM from Thermomyces lanoginosus, Lipozyme RM IM from Rhizomucor miehei, and Novozym 435 from Candida antarctica, was determined in acidolysis performed in hexane using the homologous series of even carbon number, saturated fatty acids (SFAs) of 6-22 carbons. Triolein with individual SFAs or a mixture of equimolar quantities of SFAs was used as the substrate. The effects of operating variables including the mole ratio of fatty acid to triolein, temperature, enzyme dosage, and time on incorporation were also investigated. Incorporation abilities of the enzymes tested were found to be significantly different for most of FAs at the experimental conditions evaluated. Lipases acted weakly on SFAs of which the carbon chain length was shorter than eight carbon atoms and higher than 18 carbon atoms. Lipases showed a bell-shaped distribution in incorporation vs chain length plot with a maximum around C12-C16. Among the experimental parameters tested, the effect of the substrate mole ratio was greater than those of the others, and the highest incorporation was observed for C12 (36.98%), C14 (37.63%), and C16 (38.66%) at a 4:1 substrate mole ratio with Lipozyme TL IM. Lipases caused significantly different levels of acyl migration from sn-1,3 to sn-2 positions.
Ihsan Karabulut; Gokhan Durmaz; Ali Adnan Hayaloglu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  57     ISSN:  1520-5118     ISO Abbreviation:  J. Agric. Food Chem.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2010-03-30     Completed Date:  2010-07-15     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7584-90     Citation Subset:  IM    
Department of Food Engineering, Inonu University, Malatya, Turkey.
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MeSH Terms
Ascomycota / enzymology
Candida / enzymology
Enzymes, Immobilized / chemistry
Fatty Acids / chemistry*
Fungal Proteins / chemistry*
Rhizomucor / enzymology
Substrate Specificity
Triolein / chemistry*
Reg. No./Substance:
0/Enzymes, Immobilized; 0/Fatty Acids; 0/Fungal Proteins; 112-85-6/behenic acid; 122-32-7/Triolein

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

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