Abstract
The present research was aimed to investigate the effects of sulfuric acid on the structures of gelatin polypeptides. Gelatin samples were immersed in 0.5 M sulfuric acid solution for different periods of 15, 30, 60, 120, 240, 480, 960, and 1920 s, with possible structural changes analyzed by Fourier-transform infrared spectroscopy (FT-IR). Spectra at amide I and II regions were scrutinized using the Gaussian deconvolution method for the resulting changes in the protein secondary structure. The hydrolysis process initially led to a decrease in the α-helix chain and an increase in random coil and β-sheet structures. An equilibrium was formed in degradation and these structures were sequentially turned on each other. Results revealed a correlation between the peak intensity changes of these conformations, so that the degradation process could be observed in the conversion of α-helix to random coil and β-sheet structures and vice versa, indicating the oxidation and expansion of protein structure at the onset of the degradation process.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
