화학공학소재연구정보센터
Enzyme and Microbial Technology, Vol.22, No.6, 511-519, 1998
Interesterification and acidolysis of butterfat with oleic acid by Mucor javanicus lipase : changes in the pool of fatty acid residues
Lipases have become powerful tools in the manufacture of structured fats either via randomization of their glyceride composition or incorporation of externally supplied fatty acid residues in such glycerides. The present communication reports oil changes that occurred in the fatty acid pool of anhydrous butterfat subject to interesterification and to acidolysis with oleic acid catalyzed by a commercial lipase immobilized by plain physical adsorption onto hydrophobic hollow fibers at 40 degrees C under controlled water activity. The main goal of this research effort was to engineer butterfat so as to increase its level of unsaturated fatty acid residues and concomitantly decrease its level of medium- and long-chain saturated fatty acid residues (viz. lauric and myristic acids). Although a certain degree of net hydrolysis of butterfat was as observed the triacylglycerols of butterfat subject to acidolysis were found to possess more (approximately 30% w/w) oleic acid and significantly less (8% w/w) lauric acid and less (2% w/w) myristic acid than those of the original butterfat.