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Influence of the constant heating treatment on structural and adsorption properties of myofibrillar proteins (MPs) of chicken was investigated. The results showed that heat treatment enhanced the exposure of sulfhydryl groups and improved hydrophobicity of MPs surface. Particle size distribution of MPs significantly varied depending on heat treatment duration. Also, heat treatments resulted in significant changes in the α-helix and β-sheet structures of MPs. Besides, the MPs formed larger, irregular, and cluster-like aggregates after heat treatments. Moreover, heat treatments increased viscosity and surface roughness of MPs, while zeta potential value was reduced after heat treatments. Furhthermore, binding interactions between the MPs and spices flavors signifcanlty varied relying on nature of MPs and flavor compounds, as well as heat treatments duration. Amino acid residues were interacted with flavor compounds of spices via a variety of bonds and a stable MPs-flavors complex was performed. The obtained results provide a basis for understanding structural and physicochemical changes that occur in MPs during cooking and the interactions between MPs and flavors of spices. [Display omitted] • Heating changed the conformation of chicken myofibrillar proteins (MPs). • MPs formed larger, irregular, and cluster-like aggregates after heating. • Heating enhanced binding ability of MPs with anethole, myristicin, and estragole. • MPs were binded with spices flavors via a variety of bonds. [ABSTRACT FROM AUTHOR]

[Display omitted] • FCS-MP complex was formed through hydrogen bonding and hydrophobic interactions. • Static quenching of FCS on MPs was verified. • A looser MPs gel network structure was formed after FCS addition. • The eugenol addition promoted the release of aldehyde compounds. Interactions among flavor compounds from spices (FCS) and myofibrillar proteins (MP) were investigated. Fluorescence and Fourier transform infrared spectroscopy showed that hydrogen bonding and hydrophobic interactions were the main binding forces between FCS and MP. The FCS increased the particle size and SH content of MP and caused a reduction of zeta potential from −5.23 to −6.50 mV. Furthermore, FCS could modify the binding ability of MP and aldehydes. Eugenol reduced the ability of MP to bond with aldehydes by 22.70–47.87 %. Molecular dynamics simulations demonstrated that eugenol may combat nonanal to attain binding site of amino acid residue (PHE165) and induce protein conformational changes. Electrostatic interactions and van der Waals forces within myosin-nonanal may be disrupted by these alterations, which could reduce stability of complex and cause release of nonanal. This study could provide new insights into regulating the ability of proteins to release and hold flavors. [ABSTRACT FROM AUTHOR]

[Display omitted] • Complex of EC-MP was formed through hydrogen bonding. • Addition of EC improved the rheological and gel properties of MP. • Static quenching of anethole and estragole on MP was verified. • Anethole addition reduced the binding ability of MP to decanal. This study aimed to examine how the addition of etheric compounds (EC) affects the characteristics of myofibrillar proteins (MP) and to understand underlying interaction mechanisms. Fourier transform infrared spectroscopy confirmed that the EC-MP complex was formed through hydrogen bonding. The addition of EC resulted in an increase in the α-helix content and a decrease in the β-sheet content of MP, which would promote the protein unfolding. The unfolding of MP led to aggregation and formation of larger and non-uniform particles. As a result, the exposure of negative charge on the MP surface was enhanced, and zeta potential was decreased from −5.33 mV to −7.45 mV. Moreover, the EC-induced modification of MP conformation resulted in a less rigid three-dimensional network structure of MP gel and enhanced the discharge of aldehyde compounds (C > 6). Moreover, the rheological characteristics of MP were enhanced by the suppression of protein–protein interactions due to the MP unfolding. Molecular dynamics simulations revealed that anethole reduced the binding capacity of myosin to decanal by raising its binding energy from –22.22 kcal/mol to −19.38 kcal/mol. In the meantime, anethole competed for the amino acid residue (PHE165) where myosin connects to decanal. This caused the hydrogen bonds and hydrophobic contacts between the two molecules to dissolve, altering myosin's conformation and releasing decanal. The results might be useful in predicting and controlling the ability of proteins to release and hold onto flavors. [ABSTRACT FROM AUTHOR]

Flavor is one of the most important factors that affect consumers' preference for processed meat products. This study aimed to investigate effects of heating on interaction between myofibrillar proteins (MPs) and pyrazine compounds and understand the underlying mechanisms. A combination of multispectral, molecular docking, and molecular dynamics technologies was used to achieve study's aim. Results demonstrated that MPs underwent structural reconstruction and expansion during heating, which significantly altered surface hydrophobicity and SH content. MPs' zeta potential reduced from −7.29 to −10.47 when a short heating time. Additionally, a positive correlation was found between β-sheet content and ability of MPs to adsorb pyrazine compounds. Molecular docking analysis revealed 13 binding sites for pyrazines and MPs. Furthermore, amino acid residues and pyrazine compounds were found to interact by four different forms of forces, primarily van der Waals forces, carbon‑hydrogen bonds, alkyl groups, and π-alkyl groups. Obtained results demonstrated that adequate or optimized heat treatment could expose more binding sites, hence enhancing the binding of MPs to pyrazine compounds. This study may be used to better understand how structural changes in MPs during processing affect MPs' capacity to bind flavor substances, which can help improve flavor of processed meats to encourage their consumption. [Display omitted] • Heat treatments increased the roughness of MPs. • Thirteen identical binding sites between pyrazine and MPs were identified. • Heat-treated MPs showed high binding ability to pyrazines. • The increase in β-sheet content enhanced the binding ability of MPs to pyrazines. [ABSTRACT FROM AUTHOR]

Flavor is one of the most important factors that affect consumers' preference for processed meat products. This study aimed to investigate effects of heating on interaction between myofibrillar proteins (MPs) and pyrazine compounds and understand the underlying mechanisms. A combination of multispectral, molecular docking, and molecular dynamics technologies was used to achieve study's aim. Results demonstrated that MPs underwent structural reconstruction and expansion during heating, which significantly altered surface hydrophobicity and SH content. MPs' zeta potential reduced from −7.29 to −10.47 when a short heating time. Additionally, a positive correlation was found between β-sheet content and ability of MPs to adsorb pyrazine compounds. Molecular docking analysis revealed 13 binding sites for pyrazines and MPs. Furthermore, amino acid residues and pyrazine compounds were found to interact by four different forms of forces, primarily van der Waals forces, carbon‑hydrogen bonds, alkyl groups, and π-alkyl groups. Obtained results demonstrated that adequate or optimized heat treatment could expose more binding sites, hence enhancing the binding of MPs to pyrazine compounds. This study may be used to better understand how structural changes in MPs during processing affect MPs' capacity to bind flavor substances, which can help improve flavor of processed meats to encourage their consumption. [Display omitted] • Heat treatments increased the roughness of MPs. • Thirteen identical binding sites between pyrazine and MPs were identified. • Heat-treated MPs showed high binding ability to pyrazines. • The increase in β-sheet content enhanced the binding ability of MPs to pyrazines. [ABSTRACT FROM AUTHOR]