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pH-induced changes in hydrophobicity and key amino acid exposure regulate myoglobin digestibility
Hui Liu1,2, Yaxuan Li1,2,3, Kai Shan3
1State Key Laboratory for Quality and Safety of Agro - Products, Institute of Quality Standards and Testing Technology for Agro-Products, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Abstract:
Meat processing can cause a wide range of pH variations, which in turn affect protein digestibility. The objective of this study was to elucidate the mechanism linking pH-induced structural alterations to the in vitro digestion of myoglobin. Spectroscopic techniques and molecular dynamics simulations were employed to evaluate physicochemical changes across a pH gradient. At low pH, myoglobin exhibited increased hydrophobicity, and molecular dynamics simulations indicated a higher affinity for protease binding. The protein adopted a flexible structure with increased hydrophobic amino acids exposure and weakened hydrogen bonds, collectively enhancing digestibility. These findings provide new insights into improving the digestibility of myoglobin within the gastrointestinal tract.
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