Optimized Enzymatic Hydrolysis of Olive Pomace Proteins Using Response Surface Methodology
| Autor: | Mona Fathi, Fakhri Sadat Hosseini, Reyhane Ramezani, Ladan Rashidi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Applied Food Biotechnology, Vol 9, Iss 2, Pp 79-90 (2022) |
| Druh dokumentu: | article |
| ISSN: | 2345-5357 2423-4214 |
| DOI: | 10.22037/afb.v9i2.36192 |
| Popis: | Background and objective: Olive pomace produced in the olive oil extraction process can be used as a natural source for the extraction of bioactive peptides. The objective of this study was to consider the effects of different enzymatic conditions on Olive pomace protein hydrolysis by trypsin. Material and Methods: In this study for hydrolysis optimization of extracted protein in the olive pomace, it was used Response surface method based on the Box-Behnken design. Degree of Olive pomace protein hydrolysis, amino acid profile was determined. Determination of antioxidant activities in hydrolysate was carried out by1-diphenyl-2-picryl-hydroxyl radical scavenging and Iron (II) chelating activity, as well as, for anti-proliferative activity of supernatant on MCF-7 breast cancer cells were examined. Results and Conclusion: The optimal hydrolysis conditions were as follows: time 5h, pH 8.5, and the temperature 39°C; under these conditions, the maximum degree of hydrolysis was achieved 70.62%. 1-diphenyl-2-picryl-hydroxyl radical scavenging activity and Iron (II) chelating activity of olive pomace protein hydrolysis under optimal conditions 42.26± 2.46 and 30.91± 0.26 Obtained at a concentration of 3.5 mg ml-1, respectively and the highest anti-proliferative activity of olive pomace protein hydrolysis on MCF-7 breast cancer cell was observed at a concentration of 80 mg l-1. The amino acid analysis indicates an increase in hydrophobic and aromatic amino acid in the hydrolyzed protein. These results demonstrated due to enzymatic cleavage of peptide bonds in olive pomace protein, appreciable antioxidant potential could be achieved. |
| Databáze: | Directory of Open Access Journals |
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