Investigation of the interaction between collagen and furan derivatives during the heating process via...

The flavor retention plays a critical role in the presence of rich flavor profile of meat products. However, the interaction between collagen and furan derivatives has not been previously reported. In this study, the interaction between collagen and furan derivatives during heating was investigated using multidimensional spectroscopy and gas chromatography-mass spectrometry (GC-MS). The results revealed that the collagen structure was disrupted during the heating process, causing its depolymerization and an increase in the absolute value of zeta potential. The heating treatment induced a structural transformation in the collagen from large and ordered sheets to smaller and irregular aggregates. Meanwhile, the binding ability between collagen and furan derivatives was also significantly increased during the heating process due to the increased exposure of sulfhydryl groups and a rise in surface hydrophobicity. These findings will provide valuable insights into the retention of volatile compounds in the meat products.