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- aggregation classification "C3".
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- aggregation creator person.
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- aggregation date "2010".
- aggregation format "application/pdf".
- aggregation hasFormat 1175825.bibtex.
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- aggregation language "eng".
- aggregation publisher "Food2Know ; Ghent BC".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Agriculture and Food Sciences".
- aggregation title "Stability of whey protein derived peptides upon severe protein glycation".
- aggregation abstract "Cow’s milk and dairy products are major nutrients in the human diet, especially during infancy. Though at one time whey proteins were considered as by-product of the cheese making process, nowadays, due to their wide ranging nutritional, biological, and functional properties, whey proteins are often used in food technology as low-cost protein ingredients. However, whey-protein fractions, such as β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) represent the major allergens in cow’s milk. Therefore, the use of whey proteins in food might pose a serious threat to the milk allergic consumers. It is well reported that food processing may modify the allergenicity and detectability of proteins. This can be due to hydrolysis or chemical reactions with other food components (carbohydrates, fatty acids etc), leading to modification or destruction of the allergen’s structure. Therefore, the objective of this study was in the first stage to investigate the influence of glycation on the molecular changes induced in whey proteins. This was done with a special focus on the modifications induced on the lysine residues, free amino groups, the formation of protein bound carbonyls, formation of fluorescent compounds and brown polymers and on the protein aggregation. Matrix-assisted laser desorption/ionization - time of flight mass spectrometry (MALDI-TOF MS) was used to get a better insight into the molecular changes that took place on the protein level. Unexpectedly, this study led to the identification of protein segments in the epitope region that remained unmodified during the experiments that mimic typical food processing conditions. The 57Val – Lys76 and 31Val – Arg56 from β–LG, remained unchanged disregarding the severe heating treatment in the presence of glucose and bulk proteins and they could be identified by either direct MALDI-TOF MS and MS/MS or after a more tedious separation using reversed phase chromatography. It is proposed that these peptide segments can be used as analytical targets for the development of more robust methods for the assessment of the presence of whey proteins in processed foodstuffs. Moreover, MALDI-TOF MS and MS/MS holds potential to be used as a screening tool for the identification of such stable peptides.".
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- aggregation aggregates 1175911.
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