Abstract
Retaining volatile compounds is critical for the sensory quality of smoked meat. This study investigated how glucose-induced glycation modifies chicken skin collagen and its interaction behavior with furan derivatives. During glycation, the browning index increased from 0.13 to 0.18, confirming Maillard reaction progression. Glycation decreased D50 from 136.4 to 124.4 μm and increased the absolute zeta potential from 1.74 to 4.59 mV, indicating altered aggregation behavior and surface charge. The reactive sulfhydryl content increased from 8.58 to 25.49 nmol/mg, accompanied by enhanced surface hydrophobicity and a shift from ordered structures to random coils. These structural changes were associated with changes in the headspace concentration of furan derivatives, especially 2-acetylfuran. Molecular docking suggested that hydrogen bonding and hydrophobic interactions involving ARG-1255 and TYR-1237 contributed to collagen-furan derivative interactions. These insights provide a theoretical framework for using glycation to control aroma retention in collagen-rich matrices.