Lipase-catalyzed interesterification of butterfat with rapeseed oil: new approaches for the monitoring of the reaction.

Butterfat (BF) is one main source of diet fats. However, it has been less and less well perceived due to its poor spreadability when refrigerated and cholesterol and saturated fatty acids, promoters of coronary heart diseases. Thus, consumer’s demand for healthy palatable fat spreads with good development of modified butter-based spreads. One ordinary method used by manufacturers for such modifications is enzymatic interesterification of a lipase to restructure triacylglycerides (TAG), i.e. to induce the exchange of fatty acid residues amongst glycerol backbones. This leads to changes in TAG species and in physical properties of the fat, namely in solid fat content (SFC) and in melting profile. Rapeseed oil (RO) contains a large amount of oleic acid and has significant contents of linoleic and linolenic acids, i.e. a high global content of unsaturation-rich residues. Thus, EIE of BF with RO may bring nutritional improvements to the reaction product, when compared to BF alone. The EIE of BF and canola oil (a low-erucic acid RO) catalyzed by the immobilized sn-1,3 specific Rhizopus arrhizus lipase in solvent-free batch and micro-aqueous systems, was previously studied. The aim of the present study was first to assess the evolution of chemical, physical and thermal modifications occurring during solvent-free batch EIE of BF and RO, with the use of lipozyme TL IM. The evolution of TAG profiles, interesterification degree, dropping point, solid fat content and free fatty acids was monitored during the reaction, especially during the first hours. Differential scanning calorimetry was also applied to follow the formed product. Then the establishment of relations between the DP and differential scanning calorimetry data and the interesterification degree was emphasized