Jump to Main Content
Immobilization of Phospholipase A1 and its Application in Soybean Oil Degumming
- Yu, Dianyu, Jiang, Lianzhou, Li, Zhenlan, Shi, John, Xue, Jun, Kakuda, Yukio
- journal of the American Oil Chemists' Society 2012 v.89 no.4 pp. 649-656
- calcium, calcium alginate, crosslinking, degumming, glutaraldehyde, hydrolysis, immobilized enzymes, pH, phospholipase A1, phospholipids, phosphorus, soybean oil, temperature, thermal stability, vegetable oil
- Phospholipase A1 (PLA1), or LecitaseÂ® Ultra, was immobilized on three different supports, calcium alginate (CA), calcium alginate-chitosan (CAC), and calcium alginate-gelatin (CAG), and crosslinked with glutaraldehyde. The results indicated that PLA1âCA retained 56.2% of the enzymeâs initial activity, whereas PLA1âCAC and PLA1âCAG retained 65.5 and 60.2%, respectively. Compared with free PLA1, the optimal pH of immobilized PLA1 shifted to the basic side by 0.5â1.0 pH units and the pH/activity profile range was considerably broadened. Similarly, the temperature-optima of PLA1âCAC and PLA1âCAG increased from 50 to 60Â Â°C, and their thermal stability increased with relative activities of more than 90% that covered a wider temperature range spanning 50â65Â Â°C. In a batch oil degumming process, the final residual phosphorus content was reduced to less than 10Â mg/kg with free PLA1, PLA1âCAC and PLA1âCA in less than 5, 6 and 8Â h respectively while PLA1âCAG was only able to reduce it to 15Â mg/kg in 10Â h. When the PLA1âCAC was applied in a plant degumming trial, the final residual phosphorus content was reduced to 9.7Â mg/kg with 99.1% recovery of soybean oil. The recoveries of immobilized PLA1âCAC and activity of PLA1 were 80.2 and 78.2% respectively. Therefore, it was concluded that PLA1âCAC was the best immobilized enzyme complex for the continuous hydrolysis of phospholipids in crude vegetable oils.