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.
Bai
Yong-Xiao
YX
College of Chemistry and Chemical Engineering, State Key Laboratory of Applied Organic Chemistry, Institute of Biochemical Engineering and Environmental Technology, Lanzhou University, Lanzhou 730000, PR China.
Li
Yan-Feng
YF
Yang
Yong
Y
Yi
Liu-Xiang
LX
D000818:Animals; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D017743:Equipment Reuse; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D010179:Pancreas / Q000201:enzymology; D012822:Silicon Dioxide / Q000138:chemical synthesis* / Q000737:chemistry; D013552:Swine; D013696:Temperature
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D008049:Lipase