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Lipase/acyltransferase‐catalysed interesterification of fat blends containing n ‐3 polyunsaturated fatty acids
Author(s) -
Osório Natália Melo,
Dubreucq Eric,
da Fonseca Maria Manuela R.,
FerreiraDias Suzana
Publication year - 2009
Publication title -
european journal of lipid science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 94
eISSN - 1438-9312
pISSN - 1438-7697
DOI - 10.1002/ejlt.200800109
Subject(s) - interesterified fat , chemistry , lipase , triacylglycerol lipase , hydrolysis , organic chemistry , biocatalysis , polyunsaturated fatty acid , candida antarctica , chromatography , fatty acid , catalysis , enzyme , reaction mechanism
The lipase/acyltransferase from Candida parapsilosis is an original biocatalyst that preferentially catalyses alcoholysis over hydrolysis in biphasic aqueous/organic media. In this study, the performance of the immobilised biocatalyst in the interesterification in solvent‐free media of fat blends rich in n ‐3 polyunsaturated fatty acids ( n ‐3 PUFA) was investigated. The interesterification activity of this biocatalyst at a water activity (a w ) of 0.97 was similar to that of commercial immobilised lipases at a w values lower than 0.5. Thus, the biocatalyst was further used at an a w of 0.97. Response surface modelling of interesterification was carried out as a function of medium formulation, reaction temperature (55–75 °C) and time (30–120 min). Reaction media were blends of palm stearin (PS), palm kernel oil and triacylglycerols (TAG) rich in n ‐3 PUFA (“EPAX 4510TG”; EPAX AS, Norway). The best results in terms of decrease in solid fat content were observed for longer reaction time (>80 min), lower temperature (55–65 °C), higher “EPAX 4510TG” content and lower PS concentration. Reactions at higher temperature led to final interesterified fat blends with lower free fatty acid contents. TAG with high equivalent carbon number (ECN) were consumed while acylglycerols of lower ECN were produced.