Lipase-Catalyzed Acidolysis of Menhaden Oil with Pinolenic Acid

Lipase‐catalyzed acidolysis of menhaden oil with a pinolenic acid (PLA) concentrate, prepared from pine nut oil, was studied in a solvent‐free system. The PLA concentrate was prepared by urea complexation of the FA obtained by saponification of pine nut oil. Eight commercial lipases from different s...

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Bibliographic Details
Published in:Journal of the American Oil Chemists' Society Vol. 83; no. 2; pp. 109 - 115
Main Authors: Kim, I.H, Hill, C.G. Jr
Format: Journal Article
Language:English
Published: Berlin/Heidelberg Springer‐Verlag 01-02-2006
Springer
Springer Nature B.V
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Summary:Lipase‐catalyzed acidolysis of menhaden oil with a pinolenic acid (PLA) concentrate, prepared from pine nut oil, was studied in a solvent‐free system. The PLA concentrate was prepared by urea complexation of the FA obtained by saponification of pine nut oil. Eight commercial lipases from different sources were screened for their ability to catalyze the acidolysis reaction. Two different types of structured lipids (SL) were synthesized. The first type, which has PLA residues as a primary FA residue at the sn‐1,3 positions of the TAG, was synthesized using a 1,3‐regiospecific lipase, namely, Lipozyme RM IM from Rhizomucor miehei. The second type of SL, which has PLA residues as a primary FA residue at both the sn‐1,3 and sn‐2 positions of the TAG, was synthesized using a nonspecific lipase, namely, Novozym 435 from Candida antarctica. The effects of variations in enzyme loading, temperature, and reaction time on PLA incorporation into the oil were monitored by GC analyses. The optimal temperature and enzyme loading for synthesis of the two types of SL were 50°C and 10% of the total weight of substrates for both enzymes. The optimal reaction time for the synthesis with Lipozyme RM IM was 16h, whereas the optimal reaction time for the synthesis mediated by Novozym 435 was 36 h. Pancreatic lipase‐catalyzed sn‐2 positional analyses were also carried out on the TAG samples.
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ISSN:0003-021X
1558-9331
DOI:10.1007/s11746-006-1182-2