CROSS-LINKED STABILIZATION OF ESCHERICHIA-COLI PENICILLIN-G ACYLASE AGAINST PH BY DEXTRAN-DIALDEHYDE POLYMERS

Authors
ERTAN H KAZAN D ERARSLAN A
Citation
H. Ertan et al., CROSS-LINKED STABILIZATION OF ESCHERICHIA-COLI PENICILLIN-G ACYLASE AGAINST PH BY DEXTRAN-DIALDEHYDE POLYMERS, Biotechnology techniques, 11(4), 1997, pp. 225-229
Citations number
12
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Biotechnology techniques → ACNP
ISSN journal
0951208X
Volume
11
Issue
4
Year of publication
1997
Pages
225 - 229
Database
ISI
SICI code
0951-208X(1997)11:4<225:CSOEPA>2.0.ZU;2-4
Abstract
The inactivation kinetics of Escherichia coli penicillin G acylase (PG A), and cross-linked stabilization of the enzyme by dextran-dialdehyde derivatives of molecular weights of 11500, 37000 and 71000, were simi lar from pH 2 to pH 10. Inactivation of the native and modified PGA ob eyed first order kinetics. The lowest inactivation rate constants for native and dextran-11500-dialdehyde modified PGA were 9.0 x 10(-4) and 1.5 x 10(-4) min(-1) respectively at pH 7.0. The highest pH stabiliza tion (nearly ten-fold) was obtained at pH 7.0.