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Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports

Paper ID Volume ID Publish Year Pages File Format Full-Text
25598 43583 2006 9 PDF Available
Title
Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports
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 °C. Kinetic parameters such as maximum velocity (Vmax) and the Michaelis constant (Km) 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.

Keywords
Mesoporous silica; Covalent immobilization; Functionalized support; Activity recovery
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Covalent immobilization of triacylglycerol lipase onto functionalized novel mesoporous silica supports
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 125, Issue 4, 1 October 2006, Pages 574–582
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
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