Purification and Biochemical Characterization of a Neutral Serine Protease from Trichoderma harzianum. Use in Antibacterial Peptide Production from a Fish By-Product Hydrolysate
| Autor: | Ferid Abidi, Jean-Marc Chobert, M. Nejib Marzouki, Neyssene Aissaoui, Thomas Haertlé |
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| Přispěvatelé: | Laboratory of Protein Engineering and Bioactive Molecules (LIP-MB), National Institute of Applied Sciences and Technology, Université de Carthage - University of Carthage, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Fish Proteins Antibacterial peptide Trichoderma harzianum Protein Hydrolysates medicine.medical_treatment Antibacterial peptide production [SDV]Life Sciences [q-bio] Bioengineering Peptide Applied Microbiology and Biotechnology Biochemistry Hydrolysate Fungal Proteins 03 medical and health sciences medicine Molecular Biology Purification Serine protease chemistry.chemical_classification Gel electrophoresis Trichoderma Protease biology General Medicine Protein hydrolysate biology.organism_classification Anti-Bacterial Agents 030104 developmental biology chemistry biology.protein Serine Proteases Antibacterial activity Peptides Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology Applied Biochemistry and Biotechnology, Humana Press, 2016, pp.1-15. ⟨10.1007/s12010-016-2365-4⟩ Applied Biochemistry and Biotechnology, Humana Press, 2016, 182 (2), pp.1-15. ⟨10.1007/s12010-016-2365-4⟩ |
| ISSN: | 0273-2289 |
| DOI: | 10.1007/s12010-016-2365-4⟩ |
| Popis: | This study reports the purification and biochemical characterization of an extracellular neutral protease from the fungus Trichoderma harzianum. The protease (Th-Protease) was purified from the culture supernatant to homogeneity by a three-step procedure with 14.2% recovery and 9.06-fold increase in specific activity. The purified enzyme appeared as a single protein band after sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) with a molecular mass of about 20 kDa. The optimum pH and temperature for the proteolytic activity were pH 7.0 and 40 °C, respectively. The enzyme was then investigated for its potential application in the production of antibacterial peptides. Interestingly, Scorpaena notata viscera protein hydrolysate prepared using the purified serine protease (Th-Protease) showed remarkable in vitro antibacterial activities. A peptide with a high antibacterial activity was further purified by a three-step procedure, and its sequence was identified as FPIGMGHGSRPA. The result of this study offers a promising alternative to produce natural antibacterial peptides from fish protein hydrolysate. |
| Databáze: | OpenAIRE |
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