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Structural changes imposed to whey proteins by UV irradiation in a continuous UV light reactor.
MedLine Citation:
PMID:  22630133     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 physico-chemical 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 of aromatic amino acids (i. e N-formylkynurenine and dityrosine). Furthermore, the UV induced changes in protein conformation increased the susceptibility of whey proteins to pepsin hydrolysis.
Authors:
Eleana Kristo; Artan Hazizaj; Milena Corredig
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-5-25
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  -     ISSN:  1520-5118     ISO Abbreviation:  -     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-5-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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