Abstract
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.
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Acknowledgments
This research was founded by the Chinese Higher Technology Research and Development 863 Program (2010AA101503) and the System of Soybean Industry and Technology of State Ministry of Agricultural (nycytx-004).
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Yu, D., Jiang, L., Li, Z. et al. Immobilization of Phospholipase A1 and its Application in Soybean Oil Degumming. J Am Oil Chem Soc 89, 649–656 (2012). https://doi.org/10.1007/s11746-011-1943-4
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DOI: https://doi.org/10.1007/s11746-011-1943-4