| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235743 | Process Biochemistry | 2011 | 10 Pages |
Abstract
⺠An extracellular alkaline protease (Prot-2) selectively secreted by Botrytis cinerea growing in medium containing Spirulina algae as inducer was purified. ⺠Prot-2 has a monomeric structure, is active in the pH range 5.0-9.0 and shows an optimal temperature of activity at 50 °C. Prot-2 is thermostable, and activated by Ca2+. ⺠Disulfide played a role in enzyme activity and/or stability. ⺠Prot-2 showed extreme stability towards non-ionic surfactants (5% Tween 20, 5% Triton X-100 and Nonidet P-40). ⺠It was relatively stable in 25% aqueous/organic solvent mixtures and was activated by oxidizing agents (H2O2 and sodium perborate).
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Authors
Ferid Abidi, Jean-Marc Chobert, Thomas Haertlé, Mohamed Nejib Marzouki,