Optimization of Adsorptive Immobilization of Alcohol Dehydrogenases
| Autor: | Jochen Büchs, Antje C. Spiess, Matthias Heinemann, Thomas Daussmann, Archana Harendra Trivedi |
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| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Molecular Systems Biology |
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Quality Control
yeast alcohol dehydrogenase Bioengineering Alcohol Thermoanaerobacter Thermoanaerobacter species alcohol dehydrogenase Applied Microbiology and Biotechnology protein loading chemistry.chemical_compound Adsorption Coated Materials Biocompatible Species Specificity Enzyme Stability Pressure Desiccation Alcohol dehydrogenase chemistry.chemical_classification Chromatography Lactobacillus brevis alcohol dehydrogenase biology Lactobacillus brevis Alcohol Dehydrogenase biology.organism_classification Enzymes Immobilized Yeast Enzyme Activation Lactobacillus Enzyme physical adsorption chemistry Biochemistry immobilization biology.protein Protein loading Biotechnology Protein Binding |
| Zdroj: | Journal of Bioscience and Bioengineering, 99(4), 340-347 |
| ISSN: | 1389-1723 |
| Popis: | In this work, a systematic examination of various parameters of adsorptive immobilization of alcohol dehydrogenases (ADHs) on solid support is performed and the impact of these parameters on immobilization efficiency is studied. Depending on the source of the enzymes, these parameters differently influence the immobilization efficiency, expressed in terms of residual activity and protein loading. Residual activity of 79% was achieved with ADH from bakers' yeast (YADH) after optimizing the immobilization parameters. A step-wise drying process has been found to be more effective than one-step drying. A hypothesis of deactivation through bubble nucleation during drying of the enzyme/glass bead suspension at low drying pressure (45 kPa) is experimentally verified. In the case of ADH from Lactobacillus brevis (LBADH),300% residual activity was found after drying. Hyperactivation of the enzyme is probably caused by structural changes in the enzyme molecule during the drying process. ADH from Thermoanaerobacter species (ADH T) is found to be stable under drying conditions (15 kPa) in contrast to LBADH and YADH. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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