Title of article :
A new support for the immobilization of penicillin acylase
Author/Authors :
He، نويسنده , , Jing and Li، نويسنده , , Xiaofen and Evans، نويسنده , , D.G and Duan، نويسنده , , Xue and Li، نويسنده , , Chengyue Li، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2000
Pages :
9
From page :
45
To page :
53
Abstract :
Mesoporous MCM-41 having well ordered long-range structure, large pore diameters, narrow pore-size distribution, high pore volume and specific surface area has been synthesized. The surface of MCM-41 has an abundance of weakly acidic hydroxyl groups. Assay results show that MCM-41 is a more effective support for the immobilization of Penicillin Acylase (PA) than many of other supports due to its structural and surface characteristics. PA can be immobilized on MCM-41 through either direct immobilization or covalent coupling. The former gives higher activity of IME than the later. In the direct immobilization, PA molecules are immobilized on MCM-41 through the hydrogen-bonded interaction between hydroxyl groups of MCM-41 and carbonyl or amino groups in the PA molecule.
Keywords :
Immobilization , MCM-41 , Penicillin acylase
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2000
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1715867
Link To Document :
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