Browsing by Subject "fluorescence spectroscopy"
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(2013)A review of the literature emphasised the significance of protein oxidation, which can lead to such modifications as the loss of essential amino acids and protein cross-links, and may bring about adverse effects on human nutrition and protein functionality. As the globulin fraction constitutes the predominant storage protein in oats, oxidation of oat globulin is in great need of attention and understanding. Oat globulin-containing oil-in-water emulsions were used as a food model. Thus, the objectives of the present work include the oxidation of oat proteins as well as lipid oxidation in prepared food emulsions together with a commercial oat protein-containing cream, and the possible antioxidant activities of berry phenolics (i.e. ellagitannins) towards protein oxidation. Oat globulin was extracted with a cold isolation buffer preceded by the removal of water-soluble impurities. Oxidation took place in darkness by placing the emulsion and cream samples in an oven with continuous stirring and a constant temperature at 37 oC. Sampling for lipid and protein oxidation measurements was carried out at day 0, 3 6 and 9. During the 9-day oxidation, no hexanal was detected in any oat protein-containing samples except for the ones without oat proteins, which were measured by headspace gas chromatography. The development of protein oxidation in prepared emulsions could not be revealed by the proposed loss of tryptophan fluorescence, as the tryptophan fluorescence actually increased and then decreased in the current study as opposed to continuous decrease as indicated in references, but carbonyl and dityrosine formation reflected the progression of protein oxidation. However, the same fluorescence techniques as in prepared emulsions ended up with contradictory fluorescence results in cream samples due to syneresis of oat creams during oxidation. In conclusion, fluorescence spectroscopy is a promising technique to investigate protein oxidation in food emulsions using carbonyl and dityrosine formation as oxidation markers.
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(2015)The literature review related to faba bean proteins, the mechanism of protein oxidation and detection methods for protein oxidation as well as the relationship between lipid and protein oxidation. Native faba bean, faba bean treated by oven and microwave, as well as soy protein isolate were used as materials. The materials differed in their lipoxygenase activity. Oil-in-water emulsions were made of 10% purified (removal of antioxidants) rapeseed oil and 3% water soluble proteins that were extracted from flour samples. The emulsions were prepared by homogenizing using microfludizer. Oxidation took place in the oven at 37 °C in the dark with constant stirring by magnet stirrers. Sampling for measurements was carried out on day 0, 1, 4 and 7 from each replicate. Oxidative stability of was monitored by following lipid oxidation as formation of conjugated dienes and hexanal, and by following protein oxidation by measuring loss of tryptophan, formation of carbonyls and dityrosine through fluorescence detections both in the lipid phase and in the continuous phase. In this study, the degree of protein oxidation was generally consistent with corresponding lipid oxidation. Generally, the degree of protein oxidation in lipid phase of emulsions was higher than that in continuous phase, although the protein content was far less in the lipid phase. Both results implied co-oxidative relationship between lipid and protein oxidation. In addition, the results showed that thermal treatment or microwave irradiation can not only result in retarding or decreasing lipid oxidation by lowing lipoxygenase (LOX) activity, but also affect protein oxidation via lipid oxidation and the conformational changes of proteins.
Now showing items 1-2 of 2