Influence of the spacer length on the activity of enzymes immobilised on nylon/polyGMA membranes
| Autor: | Nadia Diano, Umberto Bencivenga, M.M El-Masry, S. Di Martino, Marianna Portaccio, Damiano Gustavo Mita, A Mattei, A. De Maio |
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| Rok vydání: | 2003 |
| Předmět: |
Glycidyl methacrylate
Immobilized enzyme Process Chemistry and Technology Diffusion technology industry and agriculture Substrate (chemistry) Bioengineering Grafting Biochemistry Catalysis Isothermal process chemistry.chemical_compound Membrane chemistry Chemical engineering Polymer chemistry Bioreactor |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 21:239-252 |
| ISSN: | 1381-1177 |
| DOI: | 10.1016/s1381-1177(02)00229-1 |
| Popis: | β-Galactosidase has been immobilised through spacers of different length on nylon membranes grafted with glycidyl methacrylate. Hexamethylendiamine, ethylendiamine or hydrazine have been separately used as spacers. The behaviour of the catalytic membranes has been studied in a bioreactor operating under non-isothermal conditions as a function of the applied temperature difference ΔT. Comparison of the enzyme reaction rates under isothermal and non-isothermal conditions resulted in percentage activity increases (PAI) and reduction of the production time (τr) proportional to the size of the applied ΔT. Both these parameters increased with the increase of the spacer length. Results have been discussed in the frame of reference of the process of thermodialysis which reduces the limitations to the diffusion of substrate and reaction products across the catalytic membrane, limitations introduced by the grafting and immobilisation process. The advantages of employing non-isothermal bioreactors in biotechnological productive processes have been outlined. |
| Databáze: | OpenAIRE |
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