Some factors affecting the immobilization of penicillin G acylase on calcined layered double hydroxides

Citation
Jl. Ren et al., Some factors affecting the immobilization of penicillin G acylase on calcined layered double hydroxides, J MOL CAT B, 16(2), 2001, pp. 65-71
Citations number
11
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
16
Issue
2
Year of publication
2001
Pages
65 - 71
Database
ISI
SICI code
1381-1177(200112)16:2<65:SFATIO>2.0.ZU;2-D
Abstract
A new type of support, calcined layered double hydroxides (CLDH), has been used to immobilize penicillin G acylase. The effect of varying the composit ion of the layered double hydroxide precursor and the calcination temperatu re on the activity of the immobilized enzyme has been studied. The activity of the immobilized enzyme decreased with increasing Mg/Al molar ratio of t he CLDH. Mg/Al-CLDH had a higher affinity for the enzyme than Zn/Al-CLDH, b ut a lower percentage expressed activity. The activity of the immobilized e nzyme was a maximum when the calcination temperature was between 450 and 55 0 degreesC. The amount of enzyme adsorbed by the support shows a close corr elation with its surface area. Immobilization of the enzyme on the support increases the acid resistance of the former. (C) 2001 Elsevier Science B.V. All rights reserved.