RESULTS: Heat and UHP treatments induced the unfolding of DLp to varied degrees, as revealed by fluorescence spectroscopy, ultraviolet-visible absorption, circular dichroism spectra and surface hydrophobicity measurements. Two types of heating-denatured states with varied unfolding degrees were obtained, while UHP at both levels of 100/500 MPa caused partial unfolding of DLp and the presence of a molten-globule state, which significantly enhanced the binding affinity between DLp and (E,E)-2,4-heptadienal. In particular, significantly modified secondary structures of DLp were observed in heating-denatured samples. Excessive denaturing and unfolding degrees resulted in no significant changes in the absorption behavior of the volatile ligand, as characterized by observations of fluorescence quenching and analysis of headspace concentrations.
CONCLUSION: Defining process-induced conformational transition behavior of matrix proteins could be a promising strategy to regulate food flavor attributes and, particularly, to produce DLp coextracted with limited off-flavor components by modifying their interaction during extraction processes. © 2023 Society of Chemical Industry.
RESULTS: The yield of DFG obtained in this study was 7.01 ± 0.31%. High-performance liquid chromatography analysis indicated that the imino acid content was slightly lower for DFG compared with BG (P < 0.05). Differences in molecular size and amino acids between DFG and BG were also observed. The isoelectric points of DFG and BG were at pH 8 and 5 respectively, and the overall protein solubility of BG was higher than that of DFG. Gels prepared from BG exhibited higher bloom strength, viscosity and clarity and were darker in colour compared with DFG gels (P < 0.05). The gelling and melting points of BG were 21.8 and 29.47 °C respectively, while those of DFG were 20.5 and 27.8 °C respectively. BG exhibited slightly better emulsifying and foaming properties compared with DFG.
CONCLUSION: Although some differences between DFG and BG were observed, the disparities were small, which indicates that DFG could be exploited commercially as an alternative source of gelatin. © 2016 Society of Chemical Industry.