PURIFICATION OF PENICILLIN-G AMIDASE USING QUATERNARY AMMONIUM-SALTS AND EFFECT ON THE ACTIVITY OF THE IMMOBILIZED ENZYMES

Authors
Citation
Jp. Cardoso, PURIFICATION OF PENICILLIN-G AMIDASE USING QUATERNARY AMMONIUM-SALTS AND EFFECT ON THE ACTIVITY OF THE IMMOBILIZED ENZYMES, Bioprocess engineering, 16(4), 1997, pp. 209-218
Citations number
6
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
0178515X
Volume
16
Issue
4
Year of publication
1997
Pages
209 - 218
Database
ISI
SICI code
0178-515X(1997)16:4<209:POPAUQ>2.0.ZU;2-W
Abstract
This paper describes the purification of Penicillin G Amidase (EC 3.5. 1.11) using quaternary ammonium salts with the aim of increasing the a ctivity of immobilised enzymes prepared from the purified solutions. T wo different quaternary ammonium salts were tested with different solu tions of the enzyme. It was concluded that the quaternary ammonium sal ts used selectively precipitated the non-enzymatic protein leaving in solution practically all the enzyme resulting in a high yield of purif ication. Optimal conditions for purification using the two types of qu aternary ammonium salts were determined. Immobilisation studies were p erformed from various purified enzyme solutions, using different amoun ts of a quaternary ammonium salt. The immobilised enzymes so obtained showed a much higher activity than the immobilised enzyme obtained fro m non-purified enzyme solutions.