Observational evidence of the interaction between myofibrillar protein and polycyclic aromatic hydrocarbons as influenced by heat, ultrasound, and heat-ultrasound treatments.

Authors

Han Peng, Jiamin Shen, Changyu Zhou, Jinxuan Cao, Daodong Pan, Qiang Xia

Published in

Food research international (Ottawa, Ont.). Volume 242. Issue Pt 1. Pages 119867. Oct 31, 2026. Epub Jun 25, 2026.

Abstract

Potential exposure to polycyclic aromatic hydrocarbons (PAHs) during meat processing depends not only on total residues, but also on protein-associated retention and potential release tendency. This study examined how heat, ultrasound, and heat-ultrasound treatments remodeled lamb myofibrillar protein (MP) and altered its apparent interactions with naphthalene (Nap), anthracene (Ant), benzo[a]anthracene (BaA), and acenaphthylene (Ace). Multispectral analysis showed that physical treatments mainly induced local conformational rearrangement, as reflected by redistributed secondary structures, perturbed aromatic-residue microenvironments, and altered hydrophobic microdomain accessibility. PAH addition caused ligand-selective fluorescence quenching and local conformational adjustment. Stern-Volmer constants and bimolecular quenching rate constants ranged from 0.4575 × 10⁵ to 9.6814 × 10⁵ L mol^-1 and from 4.5750 × 10¹² to 9.6814 × 10¹³ L mol^-1 s^-1, respectively, suggesting apparent static quenching associated with ground-state complex formation. Ultrasound treatments produced ligand- and temperature-dependent shifts in quenching and binding responses. Notably, ultrasound-treated Ant at 308 K showed an apparent Ka of 2.75 × 10⁶ L mol^-1, compared with 5.66 × 10¹ L mol^-1 for untreated samples. Molecular docking predicted that all PAHs could occupy internal hydrophobic cavities of the myosin heavy chain-1 (MYH-1), with binding free energies of -5.723 to -6.6685 kcal mol^-1, supporting cavity-embedded hydrophobic association. Using Ant as a representative PAH, molecular dynamics simulation further revealed treatment-dependent changes in Ant-MYH-1 stability, flexibility, compactness, and solvent exposure. Overall, physical processing regulated PAH-MP apparent bound-state stability by reshaping hydrophobic pocket accessibility rather than uniformly strengthening binding, which may inform interpretation of PAHs retention and release in protein-rich meat matrices.

PMID:
42629089
Bibliographic data and abstract were imported from PubMed on 22 Aug 2026.

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