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- Title
Purification and Biochemical Characterization of a Neutral Serine Protease from Trichoderma harzianum. Use in Antibacterial Peptide Production from a Fish By-Product Hydrolysate.
- Authors
Aissaoui, Neyssene; Chobert, Jean-Marc; Haertlé, Thomas; Marzouki, M.; Abidi, Ferid
- Abstract
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.
- Subjects
PROTEOLYTIC enzymes; TRICHODERMA; HOMOGENEITY; GEL electrophoresis; PROTEIN hydrolysates
- Publication
Applied Biochemistry & Biotechnology, 2017, Vol 182, Issue 2, p831
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-016-2365-4