Increased thermal stability of cold-adapted esterase at ambient temperatures by immobilization on graphene oxide
| Autor: | ChangWoo Lee, Sei-Heon Jang, Hye-Shin Chung, Hae Kyung Jeong, Jinwoo Han, Heeyoung Lee |
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| Rok vydání: | 2013 |
| Předmět: |
Environmental Engineering
Pseudomonas mandelii Inorganic chemistry Oxide Bioengineering Esterase Cold adapted law.invention chemistry.chemical_compound law Pseudomonas Enzyme Stability Spectroscopy Fourier Transform Infrared Recycling Thermal stability Denaturation (biochemistry) Waste Management and Disposal chemistry.chemical_classification biology Renewable Energy Sustainability and the Environment Chemistry Graphene Esterases Temperature Oxides General Medicine Hydrogen-Ion Concentration Enzymes Immobilized biology.organism_classification Recombinant Proteins Cold Temperature Kinetics Enzyme Graphite |
| Zdroj: | Bioresource Technology. 148:620-623 |
| ISSN: | 0960-8524 |
| DOI: | 10.1016/j.biortech.2013.09.018 |
| Popis: | In this study, the effect of graphene oxide (GO) on the thermal stability of a recombinant esterase from cold-adapted Pseudomonas mandelii, rEstKp, was investigated. The complex GO-rEstKp was formed by cross-linking. Both free rEstKp and GO-rEstKp complex showed similar optimum pH and temperatures. GO-rEstKp complex exhibited enhanced thermal stability at ambient temperatures than rEstKp, which prevented the denaturation of the enzyme by hydrophilic interactions. However, the catalytic efficiency of GO-rEstKp complex was lowered to approximately 40% of that of free rEstKp. This study provides an insight into the addition of GO for industrial applications of cold-adapted enzymes at ambient temperatures. |
| Databáze: | OpenAIRE |
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