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Identification and anti-oxidative potential of Milk Fat Globule Membrane (MFGM)- derived bioactive peptides released through in vitro gastrointestinal digestion

Identification and anti-oxidative potential of Milk Fat Globule Membrane (MFGM)- derived bioactive peptides released through in vitro gastrointestinal digestion

Li, He, Guan, Kaifang Guan, Liu, Min, Jiang, Wen, Yan, Fengjuan, Zhu, Aihua and Zhou, Shaobo ORCID: 0000-0001-5214-2973 (2024) Identification and anti-oxidative potential of Milk Fat Globule Membrane (MFGM)- derived bioactive peptides released through in vitro gastrointestinal digestion. Bioorganic Chemistry (0045-2):107232. ISSN 0045-2068 (Print), 1090-2120 (Online) (doi:https://doi.org/10.1016/j.bioorg.2024.107232)

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45980_ZHOU_Identification_and_anti_oxidative_potential_of_Milk_Fat_Globule_Membrane_MFGM.pdf - Accepted Version
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Abstract

This study investigated the stability of milk fat globule membrane (MFGM) protein under simulated gastrointestinal conditions using an in vitro enzymatic digestion method. The optimal hydrolysis conditions were determined by monitoring the changes in particle size and zeta-potential of MFGM protein hydrolysates over time. Furthermore, the distribution of small molecular weight peptides with antioxidant activity was explored through DEAE-52 combined with in vitro cell experiments. Two novel antioxidant peptides (TGIIT and IITQ) were identified based on molecular docking technology and evaluated their potential scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-Azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS+) radicals. TGIIT and IITQ also demonstrated remarkable abilities in promoting mitochondrial biogenesis and activating Keap1/Nrf2 signaling pathway, which can effectively counteract skeletal muscle dysfunction induced by oxidative stress. Thus, MFGM-derived antioxidant peptides have the potential to be employed in food to regulate muscle protein metabolism and alleviate sarcopenia.

Item Type: Article
Uncontrolled Keywords: Milk fat globule membrane (MFGM); protein hydrolysates; antioxidant activity; Mmolecular docking; Keap1-Nrf2 signaling pathway
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
T Technology > TP Chemical technology
Faculty / School / Research Centre / Research Group: Faculty of Engineering & Science
Faculty of Engineering & Science > School of Science (SCI)
Last Modified: 22 Feb 2024 16:57
URI: http://gala.gre.ac.uk/id/eprint/45980

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