Solvent-free enzymatic hydrolysis of non-polar lipids in crude sunflower lecithin using phospholipase A 1 (Lecitase ® Ultra)

Abstract

In this contribution, a new chromatographic method was applied to study the hydrolysis of nonpolar lipids, i.e. triacylglicerols (TAG), diacylglycerols (DAG) and monoacylglycerols (MAG), when crude sunflower lecithin is treated with LecitaseVR Ultra, an enzymatic preparation with phospholipase A1 (PLA1) activity. Results not only proved the enzyme lipase activity toward non-polarlipids in selected reaction conditions (aqueous system, T ¼ 50 C, pH¼ 5) but also suggested the occurrence of acyl-migration phenomenon observed by other authors in similar systems. Results showed that 1 h of reaction was enough to decrease the content of TAG in 54%, while DAG and MAG concentration increased from 0.4 to 3.5 and from 1.9 to 6.5 g/100 g of crude lecithin, respectively. Along the reaction, different contents of glycerides could be achieved, obtaining products with different composition which, in combination with the presence of phospholipids (PL) and/or lysophospholipids (LPL), could present specific emulsifying/stabilizing properties with a wide range of applications in food and pharmaceutical industry.