Preparation and characterization of lipophilic antioxidative peptides derived from mung bean protein

• Published in: Food chemistry Vol. 395; p. 133535
• Main Authors: Zheng, Zhaojun, Li, Jiaxin, Chen, Yin, Sun, Hong, Liu, Yuanfa
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 30.11.2022
• Subjects: Antioxidant activity; Lipid oxidation; Lipophilic peptides; Mung bean protein hydrolysate; Structural characteristics; Lipophilic peptides; Structural characteristics; Mung bean protein hydrolysate; Antioxidant activity; Lipid oxidation
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2022.133535

[Display omitted] •Mung bean protein hydrolysate at DH 14.84% exhibited good antioxidant activity.•Hydrolysate could inhibit the lipid oxidation in emulsion, linoleic acid and sunflower oil.•Lipophilic fraction from hydrolysate was evidenced to retard lipid oxidation of bulk oil.•The 10 identified lipophilic peptides exerted their activities via forming hydrogen bonds. This study aimed to prepare and characterize antioxidative hydrolysate and its lipophilic peptides derived from mung bean protein. Our results indicated that the hydrolysate prepared with 120 min hydrolysis (MPH) possessed superb DPPH, ABTS radical scavenging activity and metal ion-chelating activity with IC50 values of 11.19 ± 0.02, 18.06 ± 0.18 and 3.78 ± 0.59 µg/mL, respectively. MPH could also effectively retard lipid oxidation for oil-in-water emulsion (up to 50%) and linoleic acid (up to 94%), as well as for bulk oil. Interestingly, the lipophilic peptide fraction (MPHP) extracted from MPH could suppress the formation of primary (up to 50%) and secondary oxidation products (up to 90%) in bulk oil. Ten lipophilic peptides identified from MPHP using LC-MS/MS possessed high amounts of hydrophobic amino acids and histidine, which might favor peptides interacting and/or forming hydrogen bonds with lipid radicals. These findings provide a new perspective for lipophilic peptides in fortifying lipids as natural antioxidants.