Solvent-free enzymatic hydrolysis of non-polar lipids in crude sunflower lecithin using phospholipase A1 (Lecitase® Ultra).

In this contribution, a new chromatographic method was applied to study the hydrolysis of non-polar lipids, i.e. triacylglicerols (TAG), diacylglycerols (DAG) and monoacylglycerols (MAG), when crude sunflower lecithin is treated with Lecitase® Ultra, an enzymatic preparation with phospholipase A1 (PLA1) activity. Results not only proved the enzyme lipase activity toward non-polar lipids in selected reaction conditions (aqueous system, T = 50 °C, pH = 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. [ABSTRACT FROM AUTHOR]