Title of article
Immobilization of penicillin G acylase on macrocellular heterogeneous silica-based monoliths
Author/Authors
Wang، نويسنده , , Hua and Jiang، نويسنده , , Yanjun and Zhou، نويسنده , , Liya and He، نويسنده , , Ying and Gao، نويسنده , , Jing، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2013
Pages
5
From page
1
To page
5
Abstract
A novel material labeled as Si(HIPEs) which possesses macroporosity and mesostructuration was synthesized and functionalized with amino or epoxy groups. The native Si(HIPEs) and functionalized Si(HIPEs) were employed as supports for penicillin G acylase (PGA) immobilization. The effect of pH and temperature on the activity of immobilized PGA was investigated. The reusability, operational stability, storage stability and kinetic properties of the immobilized PGA were examined. Compared with free PGA, the stabilities of immobilized enzyme were improved significantly, especially PGA immobilized on Amino-Si(HIPEs). The excellent reusability of the immobilized PGA will make it useful for potential commercial applications.
Keywords
Macrocellular monolith , Mesopore , Chemical modification , Immobilized PGA
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2013
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1718132
Link To Document