Abstract
The effect of the addition of lecithin hydrolysates obtained after 4- and 8-h hydrolysis by two enzymes (phospholipase A1, PLA1 and phospholipase A2, PLA2) on the stability of an emulsion comprising soybean protein isolates, sunflower oil and deionized water was investigated. The major hydrolysate obtained from the hydrolysis of lecithin by PLA1 for a duration of 4 h was 2-lysophosphatide (2-LPC), whereas the 2-LPC was further hydrolyzed to 1-lysophosphatide (1-LPC) and glycerylphosphorylcholine (GPC) when the duration of hydrolysis was increased to 8 h. Hydrolysing with PLA1 for a duration of 4 h gave the optimum concentration of 2-LPC and is the ideal hydrolysis process to use in order to obtain hydrolysates with the best emulsifying ability. The emulsion containing 2-LPC showed the best emulsifying activity and emulsion stability. By correlating the obtained results with the chemical structures of the various hydrolysates, for the first time, we found that the hydrophobic group on the sn-2 position of phosphatidylcholine (PC), which is the major component of lecithin, plays an important role in determining the emulsifying activity of PC.
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