Lipase‐mediated Acidolysis of Fully Hydrogenated Soybean Oil with Conjugated Linoleic Acid

• Published in: Journal of Food Science
• Main Authors: Ortega, J., LÓpez‐Hernandez, A., Garcia, H. S., Hill, C. G.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2004
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1111/j.1365-2621.2004.tb17860.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2621.2004.tb17860.x; http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2621.2004.tb17860.x/fullpdf

ABSTRACT: Interesterification (acidolysis) of fully hydrogenated soybean oil (melting point = 69.9 °C) with conjugated linoleic acid (CLA) was carried out in a batch reactor at 75 °C. Lipases from Candida antarctica, Rhizomucor miehei, Pseudomonas sp., and Thermomyces lanuginosus were used at 5% (wt/wt) of the total substrate load. The lipase from Rhizomucor miehei produced the fastest reaction rates, and the greatest extent of incorporation of CLA residues in acylglycerols was achieved in 12 h. Lipases from C. antarctica and T. lanuginosus produced slower initial rates, and maximum extents of incorporation of CLA residues were achieved in 24 h. The lipase from Pseudomonas sp. produced the slowest initial rate. The corresponding maximum extent of incorporation was reached in 48 h. Differential scanning calorimetry analysis of the triacylglycerol (TAG) fractions produced by C. antarctica, R. miehei , and T. lanuginosus lipases after purification by solid phase extraction showed little variation in melting point (60.4 °C, 62.8 °C, and 60.1 °C, respectively). By contrast, the corresponding TAG fraction produced by the Pseudomonas sp. lipase melted at 48.4 °C. The positional distribution of the TAGs produced by the lipase from Pseudomonas sp. differed appreciably from those produced by the other enzymes.