Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports.

A novel mesoporous silica material was synthesized via a silicate salt route in the presence of polyvinyl alcohol as the structure-directing agent under acidic conditions. The material was functionalized and employed as the supports (LPS-1 and LPS-2) for immobilizing triacylglycerol lipase from porcine pancreas (PPL). Not only they had a good thermal stability and reusability but also the activity recovery of LPS-1 and LPS-2 reached to 69% and 76%, respectively. The optimal pH and temperature region of the LPS supports immobilized PPL for hydrolysis of olive oil were at 8.0 and 55-60 degrees C. Kinetic parameters such as maximum velocity (V(max)) and the Michaelis constant (K(m)) were determined for the free and the immobilized lipase and LPS-2 immobilized PPL had the highest catalytic efficiency in the three. Meanwhile, the LPS supports exhibited many advantages than small porous materials for immobilizing PPL.