Effect of Antioxidant and Conditions on Solubility of Irradiated Food Proteins in Aqueous Solutions

Krumhar, Kim; Berry, J. W.

doi:10.1111/j.1365-2621.1990.tb01615.x

Cited by 14 publications

(6 citation statements)

References 28 publications

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“…Samples at low protein concentration irradiated at high doses showed the lowest intensity and the highest red-shift values. This finding is in accordance with reports of Brault, D'Aprano, and Lacroix (1997); Cho, Yang, and Song (1999); Kempner (2001); and Krumhar and Berry (1990) that proteins irradiated at low concentration were more affected than those irradiated at high concentration. Reactions among reactive species, which come from irradiation of water, result in different radiolytic species that may interact with protein molecules (Garrison, 1987;Yamamoto, 1992).…”

Section: Intrinsic Fluorescence Of B-lg Samples Irradiated In Solutionsupporting

confidence: 94%

Structural modifications of β-lactoglobulin subjected to gamma radiation

Hoz

Netto

2008

International Dairy Journal

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Section: Intrinsic Fluorescence Of B-lg Samples Irradiated In Solutionsupporting

confidence: 94%

Structural modifications of β-lactoglobulin subjected to gamma radiation

Hoz

Netto

2008

International Dairy Journal

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“…It was reported, that the protein in solution at low concentration is more sensitive to radiation 39, 41–43. According to Cho et al41 it is due to the greater accessibility of the radicals in a dilute solution.…”

Section: Discussionmentioning

confidence: 98%

Effects of gamma radiation on β‐lactoglobulin: Oligomerization and aggregation

et al. 2006

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The conformational changes and aggregation process of beta-lactoglobulin (beta-LG) subjected to gamma irradiation are presented. Beta-LG in solutions of different protein concentrations (3 and 10 mg/ml) and in solid state with different water activities (a(w)) (0.22; 0.53; 0.74) was irradiated using a Cobalt-60 radiation source at dose level of 1-50 kGy. Small-angle X-ray scattering (SAXS) was used to study the conformational changes of beta-LG due to the irradiation treatment. The irradiated protein was also examined by high performance size exclusion chromatography (HPSEC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing and reducing conditions and fluorescence. SAXS analysis showed that the structural conformation of irradiated beta-LG in solid state at different a(w) and dose level was essentially the same as the nonirradiated beta-LG. The scattering data also showed that the irradiation of beta-LG in solution promoted the formation of oligomers. Interestingly, from the data analysis and model building, it could be shown that the formed oligomers are linear molecules, built by linear combinations of beta-LG dimers (tetramers, hexamers, etc). The formation of oligomers was also evidenced by SDS-PAGE analysis and HPSEC chromatograms, in which products with higher molecular mass than that of the dimeric beta-LG were detected. Formation of intermolecular cross-linking between tyrosyl radicals are proposed to be at least partially responsible for this occurrence. From the results it could be shown that the samples irradiated in solution presented some conformational changes under gamma irradiation, resulting in well ordered oligomers and aggregates formed by cross-linking of beta-LG dimers subunits, while the samples irradiated in the solid state were not modified.

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“…The protein concentration affected the degree of conformational change of the irradiated proteins. In general, irradiation is more significant at a low protein concentration (Krumhar and Berry, 1990;Moon and Song, 2001). This was consistent with our observation, where at a low protein concentration, the effect of irradiation was more significant (Fig.…”

Section: Resultsmentioning

confidence: 99%

Effect of γ-Irradiation on the Molecular Properties of Myoglobin

Lee¹,

Song²

2002

BMB Reports

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To elucidate the effect of gamma-irradiation on the molecular properties of myoglobin, the secondary and tertiary structures, as well as the molecular weight size of the protein, were examined after irradiation at various irradiation doses. Gamma-irradiation of myoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, crosslinking, and aggregation of the polypeptide chains. A SDSPAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation, due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid protected against the degradation and aggregation of proteins by scavenging oxygen radicals that are produced by irradiation. A circular dichroism study showed that an increase of the irradiation decreased the alpha-helical content of myoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation increased the emission intensity that was excited at 280 nm.

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Effect of Antioxidant and Conditions on Solubility of Irradiated Food Proteins in Aqueous Solutions

Cited by 14 publications

References 28 publications

Structural modifications of β-lactoglobulin subjected to gamma radiation

Structural modifications of β-lactoglobulin subjected to gamma radiation

Effects of gamma radiation on β‐lactoglobulin: Oligomerization and aggregation

Effect of γ-Irradiation on the Molecular Properties of Myoglobin

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