KINETICS OF INVERTASE IMMOBILIZED ON POLY(PHE-LYS) COATED POLYSTYRENEBEADS

Citation
M. Mutlu et al., KINETICS OF INVERTASE IMMOBILIZED ON POLY(PHE-LYS) COATED POLYSTYRENEBEADS, Biotechnology techniques, 10(2), 1996, pp. 71-76
Citations number
17
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
0951208X
Volume
10
Issue
2
Year of publication
1996
Pages
71 - 76
Database
ISI
SICI code
0951-208X(1996)10:2<71:KOIIOP>2.0.ZU;2-#
Abstract
Surface of polystyrene beads was modified by poly(phe-lys) for inverta se immobilisation. The optimum immobilisation conditions of invertase were; 0.01% (w/v) poly(phe-lys), 2% (v/v) glutaraldehyde at 25 degrees C and pH 4.5. The kinetics of sucrose hydrolysis by free and immobili sed invertase in a batch reactor at pH 4.5 and 55 degrees C gave K-m a nd V-max values for sucrose with free and immobilised invertase of 81, 114 mM and 10.1, 9.2 mu mol glucose/min.mg enzyme, respectively. The deactivation rate constants of free and immobilised invertase were 0.0 347 and 0.0098 min(-1), respectively.