Stabilization of ficin extract by immobilization on glyoxyl agarose. Preliminary characterization of the biocatalyst performance in hydrolysis of proteins
| Autor: | Jakub F. Kornecki, Mohammed Nasreddine Zidoune, Roberto Fernandez-Lafuente, Hadjer Zaak, Oveimar Barbosa, El-Hocine Siar |
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| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Chromatography Hydrolyzed protein Immobilized enzyme 010405 organic chemistry Chemistry Substrate (chemistry) Bioengineering 01 natural sciences Applied Microbiology and Biotechnology Biochemistry 0104 chemical sciences chemistry.chemical_compound Hydrolysis Enzyme Biocatalysis 010608 biotechnology Casein Urea |
| Zdroj: | Process Biochemistry. 58:98-104 |
| ISSN: | 1359-5113 |
| Popis: | A protein extract containing ficin was immobilized on glyoxyl agarose at pH 10 and 25 °C. The free enzyme remained fully active after 24 h at pH 10. However the enzyme immobilized on the support retained only 30% of the activity after this time using a small substrate. After checking the stability of ficin preparations obtained after different enzyme-support multi-interaction times, it was found that it reached a maximum at 3 h (40-folds more stable than the free enzyme at pH 5). The immobilized enzyme was active in a wide range of pH (e.g., retained double activity at pH 10 than the free enzyme) and temperatures (e.g., at 80 °C retained three-folds more activity than the free enzyme). The activity versus casein almost matched the results using the small substrate (60%) at 55 °C. However, in the presence of 2 M of urea, it became three times more active than the free enzyme. The immobilized enzyme could be reused five cycles at 55 °C without losing activity. |
| Databáze: | OpenAIRE |
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