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Effects of strong alkali treatment on the physicochemical properties, microstructure, protein structures, and intermolecular forces in egg yolks, plasma, and granules
- Source :
- Food Chemistry. 311:125998
- Publication Year :
- 2020
- Publisher :
- Elsevier BV, 2020.
-
Abstract
- In this study we investigated the changes in the physicochemical properties, microstructure, protein structure, and intermolecular forces in egg yolk, plasma, and granule gels induced with a strong alkali. The results showed that egg yolks formed a three-dimensional gel, maintained by ionic and disulfide bonds from plasma and granules, respectively. According to spin–spin relaxation time, these gel systems fixed numerous water and lipid protons. Microstructure showed that egg yolks, plasma, and granules liberated their constituents on disruption, which randomly aggregated or bonded. Under a continuous strong alkali treatment, the second-derivative spectra of egg yolks and plasma appeared as an “aggregation band”, while the ordered structure of granules decreased. The results suggested that the aggregation of alkali-induced egg yolks formed mainly due to structural changes in plasma proteins. Granules contributed to the increased hardness and the bonding of egg yolk gels via disulfide bonds induced by alkali treatment.
- Subjects :
- food.ingredient
Ionic bonding
Alkalies
01 natural sciences
Protein Structure, Secondary
Analytical Chemistry
0404 agricultural biotechnology
food
Protein structure
Microscopy, Electron, Transmission
Yolk
Spectroscopy, Fourier Transform Infrared
Animals
Calorimetry, Differential Scanning
Chemistry
Egg Proteins
010401 analytical chemistry
Intermolecular force
Granule (cell biology)
04 agricultural and veterinary sciences
General Medicine
Alkali metal
Microstructure
Egg Yolk
040401 food science
Blood proteins
0104 chemical sciences
Chemical engineering
embryonic structures
Gels
Food Science
Subjects
Details
- ISSN :
- 03088146
- Volume :
- 311
- Database :
- OpenAIRE
- Journal :
- Food Chemistry
- Accession number :
- edsair.doi.dedup.....d16266a327866d16d2239e1cb6d124a1