title: Low molecular weight bioactive peptides derived from the enzymatic hydrolysis of collagen after isoelectric solubilization/precipitation process of turkey by-products.
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.
authors.affiliation: Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5.
authors.forename: Zied
authors.initials: Z
authors.lastname: Khiari
authors.affiliation: Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5.
authors.forename: Maurice
authors.initials: M
authors.lastname: Ndagijimana
authors.affiliation: Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5 Mirko.Betti@ales.ualberta.ca.
authors.forename: Mirko
authors.initials: M
authors.lastname: Betti
mesh_terms: D000818:Animals; D030161:Avian Proteins / Q000737:chemistry*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism*; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D010455:Peptides / Q000737:chemistry*; D011202:Poultry Products / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013381:Subtilisins / Q000737:chemistry / Q000378:metabolism; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism; D014422:Turkeys
chemical_list: D030161:Avian Proteins; D010455:Peptides; D003094:Collagen; D010450:Endopeptidases; C412470:flavourzyme; D013381:Subtilisins; D014357:Trypsin
keywords: anti-inflammatory peptide; anticholesteremic peptide; enzyme cocktail; isoelectric solubilization/precipitation; turkey collagen