Abstract
AbstractPepsin is widely used for the extraction of pepsin-solubilized collagens (PSC) from many resources. PSC-A and PSC-P were prepared from carp skin using 0.1 mol L−1 acetic acid and 0.02 mol L−1 Na2HPO4 (pH 7.2) as the dialysis solution, respectively. SDS-PAGE patterns showed PSC-A and PSC-P as type I collagens, as well as acid soluble collagen (ASC). When incubated at 40°C, no degradation was observed for ASC, but PSC-A and PSC-P were degraded into short peptides, showing lower stability than ASC. The results indicate that pepsin remaining in the PSCs resulted in their degradation, which was confirmed by the inhibition using pepstatin. This research revealed the behavior of the remaining pepsin in pepsin-solubilized collagens and an approach to the PSC stability improvement was proposed. Chromatography profiles showed that new PSC prepared by the improved method had almost the same stability as ASC.
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.
