Abstract
A process based on the isoelectric solubilization/precipitation (ISP) method was developed to recover collagen from low value poultry by-products. The application of the ISP process to turkey heads generated protein isolates and an insoluble biomass that was used to extract collagen. Isolated turkey head collagen was then enzymatically hydrolyzed for different time periods using alcalase, flavorzyme, and trypsin. The enzymatic hydrolysis approaches consisted of digesting collagen with each one of the 3 enzymes alone (alcalase, flavorzyme, or trypsin), or one of the 3 combinations of 2 enzymes (alcalase/flavorzyme, alcalase/trypsin, or flavorzyme/trypsin), or a cocktail of all 3 enzymes together (alcalase/flavorzyme/trypsin). The molecular weight distribution of turkey head collagen hydrolysates was determined using size exclusion chromatography and matrix-assisted laser desorption ionization-time of flight-mass spectrometry. The enzyme cocktail produced collagen hydrolysates with the greatest amount of low molecular weight peptides ranging from 555.26 to 2,093.74 Da. These collagen peptides showed excellent solubility over a wide pH range (2– 8) and were able to bind cholic and deoxycholic acids and significantly (P < 0.05) inhibited plasma amine oxidase in a dose- and time-dependent manner. The ISP process combined with enzyme cocktail hydrolysis represents a potential new way to produce low molecular weight bioactive collagen peptides from low value poultry by-products.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: 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.