2012
DOI: 10.1021/jf300278k
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Structural Changes Imposed on Whey Proteins by UV Irradiation in a Continuous UV Light Reactor

Abstract: 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 measureme… Show more

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Cited by 101 publications
(47 citation statements)
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“…The finding that UV-C irradiation caused less damage to proteins than thermal pasteurization agrees with a previous study conducted with whey protein solutions [37]. We have recently shown that a dosage of 4863 J/l reduces vegetative bacteria by 5-log 10 in human milk with a high total solids content without the loss of BSSL, ALP and fatty acids [29].…”
Section: Discussionsupporting
confidence: 88%
“…The finding that UV-C irradiation caused less damage to proteins than thermal pasteurization agrees with a previous study conducted with whey protein solutions [37]. We have recently shown that a dosage of 4863 J/l reduces vegetative bacteria by 5-log 10 in human milk with a high total solids content without the loss of BSSL, ALP and fatty acids [29].…”
Section: Discussionsupporting
confidence: 88%
“…The limited ability of UV light to penetrate turbid liquids has affected its use as a nonthermal technology for milk (Kristo et al, 2012). Short-wave UV light (UV-C; 200−280 nm) offers one of the most promising nonthermal continuous flow treatments that could provide milk processors with a safe, energy-efficient, and cost-effective way to gain an added measure of quality and extended shelf life due to its lethal activity against most microorganisms, including bacteria, viruses, and parasites (Bintsis et al 2000).…”
Section: Introductionmentioning
confidence: 99%
“…The knowledge of extent of the changes in composition and potential formation of undesired compounds is particularly important for regulatory approvals of novel processing methods such as UV. In a study on structural changes imposed on whey proteins by UV treatment in a continuous UV light system (Taylor-Couette-type UV system (Trojain UV, London, ON, Canada) with a 254-nm UV-C lamp and power of 3.8 W) with solutions pumped through the reactor at 30, 40, 70, 130, and 800 mL/min at the UV dose levels from 7,600 to 285 J/L, intrinsic fluorescence spectra and surface hydrophobicity measurements suggested changes in the tertiary structure of the proteins with UV exposure (Kristo et al, 2012). A study that investigated the effects of UV processing as an alternative to heat treatment of milk using a custom-made UV system (stainless steel reflector, a corrugated teflon tube coiled around a quartz sleeve with 9 UV-C lamps, 254 nm, 87 W, and UV dose of 13,870 J/L per single pass), found no major differences in terms of aroma-active compounds and flavor of milk following UV treatment, although some new volatiles and change in rheological properties were generated (Engin and Yuceer, 2012).…”
Section: Introductionmentioning
confidence: 99%
“…[45] Dityrosine formation has also been observed to occur in proteins exposed to 365 nm UV light with riboflavin,[64] and in this manuscript, but also with high energy (254 nm) UV light alone, too high for use with biologics. [65] Further, riboflavin has been used to crosslink collagen, particularly in the eye to treat keratoconus. [6668] This method relies on the same photochemistry used in this report to crosslink tyrosine residues in native collagen, and was determined to be a safe and effective method to treat keratoconus in a 1 year follow-up study.…”
Section: Resultsmentioning
confidence: 99%