Lipase-catalyzed acidolysis of butterfat with oleic acid: characterization of p...

• Author(s): Balcão, Victor M. ; Kemppinen, Asmo ; Malcata, F. Xavier ; Kalo, Paavo J.
• Date: 1998
• Persistent ID: http://hdl.handle.net/10400.14/6604
• Origin: Veritati - Repositório Institucional da Universidade Católica Portuguesa
• Subject(s): Interesterification; Immobilized lipase; Butterfat; Hollow-fiber bioreactor; Mucor circinelloides
• Document Type: Article
• Language: English

Description

The modification of anhydrous butterfat via interesterification reactions with oleic acid catalyzed by a lipase from Mucor circinelloides immobilized by adsorption onto hydrophobic hollow fibers is described. A reasonable degree of incorporation of free (externally added) oleic acid into the triacylglycerols of butterfat has been achieved while short-chain fatty acid residues remained virtually unaffected. Total saturated triacylglycerols decreased by 27%, and triacylglycerols with 32–44 acyl carbons (which contained two or three lauric, myristic, or palmitic acid residues) decreased by 33%. Total monoene and polyene triacylglycerols increased by 21% and 17%, respectively. The triacylglycerols (TAG) of interesterified butterfat had approximately 27% more oleic acid residues and approximately 8% less lauric, 6% less myristic, and 6% less palmitic acid residues than those of the original butterfat; the fraction of low-melting TAG peak increased by 19% whereas that of high-melting TAG decreased by 83%. Although a certain degree of butterfat hydrolysis was observed, enzymatic acidolysis was technically feasible and able to produce a modified butterfat with a stronger nutraceutical character.