A new support for the immobilization of penicillin acylase

Citation
H. Jing et al., A new support for the immobilization of penicillin acylase, J MOL CAT B, 11(1), 2000, pp. 45-53
Citations number
12
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
11
Issue
1
Year of publication
2000
Pages
45 - 53
Database
ISI
SICI code
1381-1177(20001130)11:1<45:ANSFTI>2.0.ZU;2-I
Abstract
Mesoporous MCM-41 having well ordered long-range structure, large pore diam eters, narrow pore-size distribution, high pore volume and specific surface area has been synthesized. The surface of MCM-41 has an abundance of weakl y acidic hydroxyl groups. Assay results show that MCM-41 is a more effectiv e support for the immobilization of Penicillin Acylase (PA) than many of ot her supports due to its structural and surface characteristics. PA can be i mmobilized on MCM-41 through either direct immobilization or covalent coupl ing. 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. (C) 2000 Elsevier Science B.V. All rights reser ved.