Lipase-catalyzed acidolysis of butterfat with oleic acid: Characterization of process and product

• Type: Article in International Scientific Journal
• Date: 1998

Authors

Balcao, VM (Author) Other; Kemppinen, A (Author) Other; F. Xavier Malcata (Author) Other; Kalo, PJ (Author) Other

Journal

Title: Enzyme and Microbial Technology

Vol. 23

Pages: 118-128

ISSN: 0141-0229

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 20 Citations

Scopus - 26 Citations

Other information

Authenticus ID: P-001-7HP

DOI: 10.1016/s0141-0229(98)00031-3

Abstract (EN): 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 of 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. (C) 1998 Elsevier Science Inc.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11