| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1188022 | Food Chemistry | 2010 | 7 Pages |
The partial hydrolysis of soybean oil, as catalysed by phospholipase A1 (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 A1 (Lecitase Ultra) were 6.8 and 40 °C, respectively. Phospholipase A1 (Lecitase Ultra) displayed good stability over a range of pH values from 4.7 to 7.4, and at temperatures below 60 °C. Phospholipase A1 (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 A1 (Lecitase Ultra). Alternative TAG hydrolysis routes for phospholipase A1 (Lecitase Ultra) are postulated, and several reaction equilibrium and rate constants were determined.
