Immobilized invertase studies on glass–ceramic support from coal fly ashes
| Autor: | P.J. Rolim Neto, Valder N. Freire, Jeckson Luiz da Silva, Benildo Sousa Cavada, A.V.P. Albertini, Ricardo Pires dos Santos, J. L. Lima Filho, Jorge Luiz Martins, Pabyton Gonçalves Cadena, Ana Lúcia Figueiredo Porto, M.C.B. Pimentel, Cosme Rafael Martínez |
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| Rok vydání: | 2013 |
| Předmět: |
Glass-ceramic
Chromatography business.industry General Chemical Engineering chemistry.chemical_element Initial activity General Chemistry Activation energy Zinc Industrial and Manufacturing Engineering law.invention Invertase chemistry law Covalent bond Environmental Chemistry Coal Sucrose hydrolysis business Nuclear chemistry |
| Zdroj: | Chemical Engineering Journal. 214:91-96 |
| ISSN: | 1385-8947 |
| DOI: | 10.1016/j.cej.2012.10.029 |
| Popis: | Invertase was covalently immobilized on new coal fly ashes glass-ceramic support with zinc sulfate (GCS Zn ). The coupling process of proteins was demonstrated by X-ray diffraction (XRD). There was no change in the optimum pH (4.6) but optimum temperature increased from 55 °C for free invertase to 60 °C for immobilized derivative. The activation energy decreased after immobilization (37.31 ± 3.40 kJ/mol) in spite of free invertase (51.34 ± 5.21 kJ/mol). There was an improvement in the Michaelis–Menten constant for sucrose hydrolysis after immobilization being 15 times lower compared to that for free invertase (0.30 ± 0.01 mmol). After ten reuses at 25 ± 2 °C, the immobilized invertase lost only 9% of initial activity, but at the optimum temperature (60 °C), the activity decrease was about 70%, what it is economically feasible under energetic view point for industrial application. |
| Databáze: | OpenAIRE |
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