| Structural changes imposed to whey proteins by UV irradiation in a continuous UV light reactor. | |
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MedLine Citation:
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PMID: 22630133 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Eleana Kristo; Artan Hazizaj; Milena Corredig |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-5-25 |
Journal Detail:
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Title: Journal of agricultural and food chemistry Volume: - ISSN: 1520-5118 ISO Abbreviation: - Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-5-28 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0374755 Medline TA: J Agric Food Chem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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