Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor.
The objective of this study was to investigate the structural changes of whey proteins during exposure in a continuous-flow UV reactor. Varying UV irradiation dosages were obtained by controlling the flow rate and the mixing speed. Whey protein isolate (WPI) solutions at concentrations of 1% and 5% (w/v) were circulated at flow rates ranging from 30 to 800 mL·min(-1), and changes in physicochemical properties of the proteins were investigated. Intrinsic fluorescence spectra and surface hydrophobicity measurements suggested changes in the tertiary structure of the proteins with UV exposure. The UV treatment also increased the concentration of total and accessible thiol groups in 1% WPI solutions, while no change was measured in 5% WPI solutions. Size-exclusion chromatography demonstrated the formation of UV-induced aggregates and oxidation products (N-formylkynurenine and dityrosine) of aromatic amino acids. Furthermore, the UV-induced changes in protein conformation increased the susceptibility of whey proteins to pepsin hydrolysis.
Department of Food Science, University of Guelph, Guelph, Ontario, Canada. ekristo@uoguelph.ca
Eleana
E
Kristo
Artan
A
Hazizaj
Milena
M
Corredig
D055598:Chemical Phenomena; D002850:Chromatography, Gel; D006868:Hydrolysis; D008894:Milk Proteins / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects*; D010434:Pepsin A / Q000378:metabolism; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014466:Ultraviolet Rays; D000067816:Whey Proteins
D008894:Milk Proteins; D000067816:Whey Proteins; D010434:Pepsin A