| Autor: |
Nalok, Dutta, Malay K, Saha |
| Rok vydání: |
2018 |
| Předmět: |
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| Zdroj: |
Methods in enzymology. 609 |
| ISSN: |
1557-7988 |
| Popis: |
Catalyst-mediated bioprocessing at an industrial scale is dependent on the sustained stability and activity of the biocatalyst. Here, we demonstrate that strategy employed to increase the stability and activity of a mesophilic lipase immobilized on graphene oxide (GO). The protein adsorption capacity of GO is much higher than of other large surface area carbonaceous materials. Its structure and physicochemical properties are reported beneficial for enzymatic activity modifications. A purified lipase from Brevibacillus borstelensis NLIP05 immobilized on GO showed remarkable increase in thermostability (at 95°C) over a broad alkaline pH range (pH 7-12) compared to the free enzyme. Thermodynamic analysis of the GO-lip showed decreases in K |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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