| Title : Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports - Bai_2006_J.Biotechnol_125_574 |
| Author(s) : Bai YX , Li YF , Yang Y , Yi LX |
| Ref : J Biotechnol , 125 :574 , 2006 |
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Abstract :
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. |
| PubMedSearch : Bai_2006_J.Biotechnol_125_574 |
| PubMedID: 16697482 |
Bai YX, Li YF, Yang Y, Yi LX (2006)
Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports
J Biotechnol
125 :574
Bai YX, Li YF, Yang Y, Yi LX (2006)
J Biotechnol
125 :574