Abstract
The partial hydrolysis of soybean oil, as catalysed by phospholipase A 1 (Lecitase Ultra) in a solvent-free system, was investigated in this study. The optimal pH and temperature for the partial hydrolysis of soybean oil by phospholipase A 1 (Lecitase Ultra) were 6.8 and 40 °C, respectively. Phospholipase A 1 (Lecitase Ultra) displayed good stability over a range of pH values from 4.7 to 7.4, and at temperatures below 60 °C. Phospholipase A 1 (Lecitase Ultra) is postulated to possess sn-1,3-position regiospecificity towards triacylglycerols (TAGs), based on the identification of the fatty acids released from TAGs following partial hydrolysis by swine pancreatic lipase (SPL) and phospholipase A 1 (Lecitase Ultra). Alternative TAG hydrolysis routes for phospholipase A 1 (Lecitase Ultra) are postulated, and several reaction equilibrium and rate constants were determined.
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