摘要
Both thermal treatment and glycation modification can induce conformational changes in collagen. • Conformationally altered collagen strongly enhances adsorption of key furanic flavor compounds from sugar smoking. • Hydrogen bonding and hydrophobic interactions dominate the binding between glycated collagen and furanic compounds. • Stable hydrogen bonds and van der Waals forces between glucose and collagen reveal atomic-scale modification mechanism. Flavor retention critically determines the sensory quality of meat products. However, how glycated collagen retains flavor compounds during heating is unclear. In this study, multidimensional spectroscopic techniques, molecular docking, and methods for structural and functional characterization were employed to investigate how glycosylated collagen affects the adsorption of furan-based aroma compounds during thermal processing. Molecular docking revealed stable hydrogen bonds and van der Waals interactions between glucose and collagen, explaining structural changes. With longer heating, the levels of four free furan derivatives decreased, indicating better collagen adsorption. This phenomenon is driven by the combined effects of thermal treatment and glycation: heating induces a conformational transition of glycated collagen from α -helices and β -sheets to random coils, accompanied by the disruption of hydrogen bonds that stabilize the native structure. These structural changes are associated with an increase in absolute zeta potential, particle size decreased, internal sulfhydryl groups were exposed, and surface hydrophobicity increased. As a result, the porosity of the collagen matrix increases, thereby improving its affinity for flavor compounds. These findings offer a theoretical foundation for optimizing flavor retention in processed meats. Download: Download high-res image (238KB) Download: Download full-size image
危险品化学品经营许可证(带存储)