Immobilization of lipases onto the halogen & haloalkanes modified SBA-15: Enzymatic activity and glycerolysis performance study.

In this study, SBA-15 was modified by halogen & haloalkanes and later used to immobilize lipases. The hydrolysis activity and the glycerolysis performance of the immobilized lipases was carefully studied. Highest activity of the immobilized Candida antarctica lipase B (CALB), Lipase from Aspergillus oryzae (AOL), Lecitase® Ultra (LU) and lipase from Rhizomucor miehei (RML) was respectively at 5577, 12000, 2822 and 11,577 U/g; in addition, the highest activity was obtained from the lowest or moderate lipase loading, at 25.73, 90.72, 89.52 and 30.56 mg/g respectively. The mechanism of lipase immobilization was studied and it was through interfacial activation. The halogen & haloalkanes modification of SBA-15 afforded considerable glycerolysis activity for diacylglycerols (DAG) preparation. CALB@SBA-15-CH 2 CH 2 (CF 2 ) 5 CF 3 and CALB@SBA-15-CH 2 CH 2 (CF 2 ) 7 CF 3 were suitable for DAG production, they both exhibited good reusability in glycerolysis reaction, with 117.36% and 93.06% of their initial glycerolysis activity retained respectively after ten cycles of reuse. The relationships between temperature with triacylglycerols (TAG) conversion were lnV 0  = 3.13-3.07/T and lnV 0  = 7.90-4.64/T respectively for CALB@SBA-15-CH 2 CH 2 (CF 2 ) 5 CF 3 and CALB@SBA-15-CH 2 CH 2 (CF 2 ) 7 CF 3 ; in addition, their activation energy (Ea) was respectively at 25.50 and 38.54 kJ/mol.

Competing Interests: Declaration of competing interest The authors have declared no conflict of interest.

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