Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles
The interaction and adsorption of enzyme, glucose oxidase (GOx), on poly(methyl methacrylate)-bovine serum albumin (PMMA-BSA) particles were studied by using a quartz crystal microbalance with dissipation (QCM-D) and laser light scattering (LLS). The enzyme was irreversibly immobilized on the PMMA-B...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 25(2009), 23 vom: 01. Dez., Seite 13456-60 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Serum Albumin, Bovine 27432CM55Q Polymethyl Methacrylate 9011-14-7 Glucose Oxidase EC 1.1.3.4 |
| Zusammenfassung: | The interaction and adsorption of enzyme, glucose oxidase (GOx), on poly(methyl methacrylate)-bovine serum albumin (PMMA-BSA) particles were studied by using a quartz crystal microbalance with dissipation (QCM-D) and laser light scattering (LLS). The enzyme was irreversibly immobilized on the PMMA-BSA particle surface. The amount of enzyme immobilized on PMMA-BSA particles and the enzymatic activity were determined by UV/vis measurements. The influences of pH and ionic strength on the adsorption indicate that the electrostatic interaction plays a major role on the immobilization. The adsorbed GOx can retain at least 80% of the free enzyme activity. Thermal stability studies reveal that the adsorbed GOx only losses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50 degrees C for 35 h |
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| Beschreibung: | Date Completed 01.02.2010 Date Revised 16.11.2017 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la9019124 |