Immobilization of a recombinant esterase from Lactobacillus plantarum on polypropylene Accurel MP1000
| Autor: | Fábio Cristiano Angonesi Brod, Willian Alexandre Suguino, Ana Carolina Maisonnave Arisi, Deise Juliana Kolling |
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| Rok vydání: | 2010 |
| Předmět: |
Immobilized enzyme
Gene Expression Bioengineering Polypropylenes Applied Microbiology and Biotechnology Biochemistry Esterase law.invention Adsorption law Escherichia coli Molecular Biology Incubation chemistry.chemical_classification Chromatography biology Esterases Temperature Substrate (chemistry) General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzymes Immobilized Recombinant Proteins Butyrates Enzyme chemistry Recombinant DNA Lactobacillus plantarum Biotechnology |
| Zdroj: | Applied biochemistry and biotechnology. 163(2) |
| ISSN: | 1559-0291 |
| Popis: | A recombinant esterase from Lactobacillus plantarum was immobilized on hydrophobic support polypropylene Accurel MP1000 by adsorption. Adsorption efficiency was 83%, and the immobilized protein was 12.4 mg/g of support. Esterase activity was determined using p-nitrophenyl butyrate as substrate, and highest activities were observed at 50 °C for immobilized enzyme and 30 °C for free enzyme extract. Concerning thermal stability, after enzyme incubation at 80 °C for 30 min, immobilized and free enzyme retained 91% and 56% of initial activity, respectively. Immobilized enzyme presented lower V(max) and higher K(m) than free enzyme. Protein was not released from the support, and esterase activity increased after 3 cycles of reuse. |
| Databáze: | OpenAIRE |
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