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Immobilization of Phospholipase A1 and its Application in Soybean Oil Degumming

Author:
Yu, Dianyu, Jiang, Lianzhou, Li, Zhenlan, Shi, John, Xue, Jun, Kakuda, Yukio
Source:
journal of the American Oil Chemists' Society 2012 v.89 no.4 pp. 649-656
ISSN:
0003-021X
Subject:
calcium, calcium alginate, crosslinking, degumming, glutaraldehyde, hydrolysis, immobilized enzymes, pH, phospholipase A1, phospholipids, phosphorus, soybean oil, temperature, thermal stability, vegetable oil
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.
Agid:
448352