pH-induced changes in hydrophobicity and key amino acid exposure regulate myoglobin digestibility.

Hui Liu, Yaxuan Li, Kai Shan, Chunbao Li, Xiaoyan Tang

Abstract read

In one paragraph

Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Hui LiuState 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.

Yaxuan LiState 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.

Kai ShanState Key Laboratory of Meat Quality Control and Cultured Meat Development, MOST; Key Laboratory of Meat Processing, MARA; Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control; College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.

Chunbao LiState Key Laboratory of Meat Quality Control and Cultured Meat Development, MOST; Key Laboratory of Meat Processing, MARA; Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control; College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.

Xiaoyan TangState 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.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

DigestibilityHeme cavityHydrophobicityIn vitro digestionMyoglobin

Identifiers

PMID42179951

DOI10.1016/j.fochx.2026.103948

PMCPMC13197811

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.