| Literature DB >> 32871354 |
Tsun-Thai Chai1, Jianbo Xiao2, Sharmila Mohana Dass3, Jia-Yun Teoh3, Kah-Yaw Ee1, Wen-Jie Ng1, Fai-Chu Wong4.
Abstract
Jackfruit is a sweet tropical fruit with very pleasant aroma, and the ripe seeds are edible. In this study, jackfruit seed proteins were isolated and subjected to trypsin digestion. The resultant protein hydrolysate was then subjected to antioxidant assay-guided purification, using centrifugal filtration, C18 reverse-phase and strong cation exchange (SCX) fractionations. The purified SCX fraction was further analyzed by de novo peptide sequencing, and two peptide sequences were identified and synthesized. Peptide JFS-2 (VGPWQK) was detected with antioxidant potential, with EC50 value comparable to that of commercial GSH antioxidant peptide. Additionally, the identified peptides were tested with protein protection potential, in an albumin protein denaturation inhibitory assay. Concurrently, we also investigated the pH, temperature, and gastrointestinal-digestion stability profiles for the identified peptide. With further research efforts, the identified peptides could potentially be developed into preservative agent for protein-rich food systems or as health-promoting diet supplements.Entities:
Keywords: Antioxidant peptide; Arginine; Artocarpus heterophyllus; Diet supplement; Electrostatic interaction; Hydrogen bond; Hydrophobicity; Synergistic
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Year: 2020 PMID: 32871354 DOI: 10.1016/j.foodchem.2020.127876
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514