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Characterization of antioxidant peptides from Thai traditional semi-dried fermented catfish
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Metadata
Document Title
Characterization of antioxidant peptides from Thai traditional semi-dried fermented catfish
Author
Chaijan M., Rodsamai T., Charoenlappanit S., Roytrakul S., Panya A., Phonsatta N., Cheong L.-Z., Panpipat W.
Name from Authors Collection
Affiliations
Food Technology and Innovation Research Center of Excellence, School of Agricultural Technology and Food Industry, Walailak University, Nakhon Si Thammarat, 80160, Thailand; Functional Proteomics Technology Laboratory, Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Bangkok, 12120, Thailand; Food Biotechnology Research Team, Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency, Bangkok, 12120, Thailand; Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition, College of Food and Pharmaceutical Science, Ningbo University, Ningbo, 315211, China
Type
Article
Source Title
Fermentation
ISSN
23115637
Year
2021
Volume
7
Issue
4
Open Access
Gold
Publisher
MDPI
DOI
10.3390/fermentation7040262
Abstract
Herein, the antioxidant peptides from a Thai traditional semi-dried fermented farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) catfish, Pla Duk Ra, were characterized. After extraction and deproteinization, Pla Duk Ra crude peptide extract (CPE) was fractioned using 2 connected Hitrap Sephadex-G25 columns, yielding two significant fractions, F1 with higher browning intensity (A420) and F2. CPE, F1, and F2 had different amino acid profiles, contents, and sequences evaluated by LC-MS/MS, which could be responsible for their antioxidant properties. F2 contained the highest numbers of hydrophobic amino acid (HBA) (47.45%) and aromatic amino acid (27.31%), followed by F1, and CPE. The peptides with 8–24 amino acid residues were detected in CPE and its fractions. In CPE, F1, and F2, there were 69, 68, and 85 peptides with varied HBA content, respectively. ARHSYGMLYCSCPPND (50% HBA), ALRKMGRK (37.5% HBA), and ANWMIPLM (87.5% HBA) were the most prevalent peptides found in CPE, F1, and F2. Overall, F2 was the most effective at inhibiting free radicals (DPPH• and ABTS•+) and reactive oxygen species (hydroxyl radical, singlet oxygen, and hydrogen peroxide), followed by F1 and CPE. The metal chelation of F1 was, however, superior to that of F2 and CPE. For the stability test, the effects of pH, heating temperature, and in vitro digestion on the DPPH• scavenging activity of F2 were investigated. The activity was boosted by lowering the pH and raising the heating temperature. In the gastrointestinal tract model system, however, roughly 50% of DPPH• scavenging activity reduced after digesting. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
Keyword
Antioxidant | Catfish | Lipid oxidation | Peptide | Traditional fermented fish
License
CC BY
Rights
Author
Publication Source
Scopus
Note
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