Back to Search
Start Over
Active site titration of immobilized beta-galactosidase for the determination of active enzymes.
- Source :
-
Biochemical Engineering Journal . Jan2015, Vol. 93, p137-141. 5p. - Publication Year :
- 2015
-
Abstract
- In the present study, an active site titration method is demonstrated, to determine the amount of active enzyme (β-galactosidase), immobilized on a support. Two types of supports were investigated, viz. amino acrylic resin and a mixed matrix membrane. Furthermore, 2′,4′-dinitrophenyl 2-deoxy-2-fluoro-β- d -galactopyranoside was used as an inhibitor for the active site titration of immobilized β-galactosidase obtained from Kluyveromyces lactis . Using the active site titration, approximately 8.3 mg of active enzyme was found on 1 g of dried commercially available SPRIN imibond, which is an amino acrylic resin with covalently bound β-galactosidase obtained from K. lactis . However, this method, in its present form, was not effective on the mixed matrix membranes due to the irreversible partial adsorption of the leaving group (2′,4′-dinitrophenolate) by the membrane. This observation implied that it is important to investigate interactions between the support and the used inhibitor and leaving group. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 1369703X
- Volume :
- 93
- Database :
- Academic Search Index
- Journal :
- Biochemical Engineering Journal
- Publication Type :
- Academic Journal
- Accession number :
- 99828736
- Full Text :
- https://doi.org/10.1016/j.bej.2014.10.007