Immobilization of Phospholipase A1 and its Application in Soybean Oil Degumming

摘要

Phospholipase A1 (PLA1), or Lecitase® 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 PLA1–CA retained 56.2% of the enzyme’s initial activity, whereas PLA1–CAC and PLA1–CAG retained 65.5 and 60.2%, respectively. Compared with free PLA1, the optimal pH of immobilized PLA1 shifted to the basic side by 0.5–1.0 pH units and the pH/activity profile range was considerably broadened. Similarly, the temperature-optima of PLA1–CAC and PLA1–CAG increased from 50 to 60 °C, and their thermal stability increased with relative activities of more than 90% that covered a wider temperature range spanning 50–65 °C. In a batch oil degumming process, the final residual phosphorus content was reduced to less than 10 mg/kg with free PLA1, PLA1–CAC and PLA1–CA in less than 5, 6 and 8 h respectively while PLA1–CAG was only able to reduce it to 15 mg/kg in 10 h. When the PLA1–CAC was applied in a plant degumming trial, the final residual phosphorus content was reduced to 9.7 mg/kg with 99.1% recovery of soybean oil. The recoveries of immobilized PLA1–CAC and activity of PLA1 were 80.2 and 78.2% respectively. Therefore, it was concluded that PLA1–CAC was the best immobilized enzyme complex for the continuous hydrolysis of phospholipids in crude vegetable oils.