| Fatty acid selectivity of lipases during acidolysis reaction between triolein and saturated fatty acids varying from caproic to behenic acids. | |
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MedLine Citation:
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PMID: 19645505 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Ihsan Karabulut; Gokhan Durmaz; Ali Adnan Hayaloglu |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of agricultural and food chemistry Volume: 57 ISSN: 1520-5118 ISO Abbreviation: J. Agric. Food Chem. Publication Date: 2009 Aug |
Date Detail:
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Created Date: 2010-03-30 Completed Date: 2010-07-15 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0374755 Medline TA: J Agric Food Chem Country: United States |
Other Details:
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Languages: eng Pagination: 7584-90 Citation Subset: IM |
Affiliation:
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Department of Food Engineering, Inonu University, Malatya, Turkey. ikarabulut@inonu.edu.tr |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Ascomycota
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enzymology Candida / enzymology Enzymes, Immobilized / chemistry Fatty Acids / chemistry* Fungal Proteins / chemistry* Hydrolysis Rhizomucor / enzymology Stereoisomerism Substrate Specificity Triolein / chemistry* |
| Chemical | |
Reg. No./Substance:
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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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