title: Fatty acid selectivity of lipases during acidolysis reaction between triolein and saturated fatty acids varying from caproic to behenic acids.
abstract: 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.
authors: Department of Food Engineering, Inonu University, Malatya, Turkey. ikarabulut@inonu.edu.tr
authors: Ihsan
authors: I
authors: Karabulut
authors: Gokhan
authors: G
authors: Durmaz
authors: Ali Adnan
authors: AA
authors: Hayaloglu
mesh_terms: D001203:Ascomycota / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry; D005227:Fatty Acids / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D006868:Hydrolysis; D020103:Rhizomucor / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity; D014304:Triolein / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D005227:Fatty Acids; D005656:Fungal Proteins; D014304:Triolein; C007547:behenic acid