2017
DOI: 10.1080/10942912.2016.1233429
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Color and gelling properties of dried egg white: Effect of drying methods and storage conditions

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Cited by 28 publications
(17 citation statements)
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“…Literature data states that the type of the drying process, temperature and the type of proteins and gums used affects the porosity and, therefore, the final result of the drying process (Sundaram and Durance, , Begum et al, ). In this study, on one hand, drying could have caused a change in protein conformation, as reported by Katekhong and Charoenerin (), which subsequently affected porosity and reconstitution properties. On the other hand, the presence of galactommanans and their structural changes during drying could have affected the reconstitutution properties.…”
Section: Resultssupporting
confidence: 55%
“…Literature data states that the type of the drying process, temperature and the type of proteins and gums used affects the porosity and, therefore, the final result of the drying process (Sundaram and Durance, , Begum et al, ). In this study, on one hand, drying could have caused a change in protein conformation, as reported by Katekhong and Charoenerin (), which subsequently affected porosity and reconstitution properties. On the other hand, the presence of galactommanans and their structural changes during drying could have affected the reconstitutution properties.…”
Section: Resultssupporting
confidence: 55%
“…Wu [30] reported that peroxyl radicals generated during the processing could react with the sulfhydryl groups to form sulphinyl radicals and decrease the free SH groups in egg white. Katekhong and Charoenrein [17] also observed a lower level of total SH groups and a higher level of exposed SH groups in egg white.…”
Section: Surface Tension and Sh Groupsmentioning
confidence: 87%
“…The egg white was measured for SH groups (total SH groups and exposed SH groups) using Ellman's reagent (5,5'-dithiobis 2-nitrobenzoic acid; DTNB) [17] . For measuring the exposed SH groups, 5 mL of egg white was added to 5 mL of Tris-glycine buffer (pH 8) containing 0.1 M Tris, 0.1 M glycine, and 4 mM EDTA.…”
Section: Determination Of Sh Groupsmentioning
confidence: 99%
“…The thermal stability of the protein is associated with its amino acid composition, protein has high content of hydrophobic amino acids usually presents better thermal stability. [36] Enzymatic hydrolysis could break the globular structure of OVA, increase hydrophobic groups of protein and show higher thermal stability. After glycation, thermal denaturation temperature increased, which indicates the enhanced resistance against thermal denaturation after glycation.…”
Section: Resultsmentioning
confidence: 99%