Immobilization of Candida antarctica lipase B onto SBA-15 and their application in glycerolysis for diacylglycerols synthesis

• Thermal stability of the immobilized CALB was greatly influenced by water content.
• 53.6 wt% of diacylglycerols was obtained from SBA-15-CALB mediated glycerolysis.
• SBA-15 with small pore diameter showed better operational stability for SBA-15-CALB.

In this study, Candida antarctica lipase B (CALB) was immobilized on SBA-15 with three pore diameters. CALB loading was found increased with CALB concentration increasing from 20.3 to 80.12 μg/ml. Higher CALB loading was observed from SBA-15 with pore diameters at 8.1 nm (SBA-15(8.1)), yet highest hydrolytic activity was found at SBA-15(12.5). Thermal stability of the immobilized CALB (SBA-15-CALB) samples was greatly influenced by their water content, after 4 h storage at 70 °C, 8.93 and 67.4% of the initial activity was observed from SBA-15-CALB samples with water content at 9.23 and 3.22% respectively. The SBA-15-CALB samples were then used in glycerolysis of corn oil, and 53.6 wt% of diacylglycerols was obtained after optimization. The operational stability was tested, and after 5 consecutive applications, 92.5 and 80.3% of the initial glycerolysis activity was remained respectively from SBA-15(6.6)-CALB and SBA-15(12.5)-CALB.