Microstructure change in whole egg protein aggregates upon freezing: Effects of freezing time and sucrose addition. (May 2021)
- Record Type:
- Journal Article
- Title:
- Microstructure change in whole egg protein aggregates upon freezing: Effects of freezing time and sucrose addition. (May 2021)
- Main Title:
- Microstructure change in whole egg protein aggregates upon freezing: Effects of freezing time and sucrose addition
- Authors:
- Fang, Bowen
Isobe, Kazuhiro
Handa, Akihiro
Nakagawa, Kyuya - Abstract:
- Abstract: Protein is not stable under freezing conditions, which may lead to changes in protein aggregates. In this study, liquid whole egg samples were frozen and thawed. The structural changes in the whole egg aggregates were then analyzed. After analyzing samples using tunable resistance pulse sensing, it was found that the number of protein aggregate samples increased nearly six-fold after freezing and thawing. The addition of sucrose reduced the enhancement of particle number. The surface characteristics of whole egg protein aggregates varied during the freezing process. By adding sucrose to the whole egg sample, the variation in aggregate surface characteristics was weakened. The same samples were also investigated using a small-angle X-ray scattering device. The results showed that the inner structure of whole egg protein aggregates became less packed during the freezing process. However, changes in protein aggregates caused by freezing were prevented by the addition of sucrose. In conclusion, freezing unfolded whole egg proteins and reduced protein solubility, which further increased the number of protein aggregates and changed the structure of the aggregates. Sucrose could be a cryoprotectant and inhibit the influence of freezing on whole egg protein aggregates. Highlights: Aggregate formation upon freezing of the whole egg solution was investigated. It found that the particle number concentration increased during the freezing process. The aggregates became lessAbstract: Protein is not stable under freezing conditions, which may lead to changes in protein aggregates. In this study, liquid whole egg samples were frozen and thawed. The structural changes in the whole egg aggregates were then analyzed. After analyzing samples using tunable resistance pulse sensing, it was found that the number of protein aggregate samples increased nearly six-fold after freezing and thawing. The addition of sucrose reduced the enhancement of particle number. The surface characteristics of whole egg protein aggregates varied during the freezing process. By adding sucrose to the whole egg sample, the variation in aggregate surface characteristics was weakened. The same samples were also investigated using a small-angle X-ray scattering device. The results showed that the inner structure of whole egg protein aggregates became less packed during the freezing process. However, changes in protein aggregates caused by freezing were prevented by the addition of sucrose. In conclusion, freezing unfolded whole egg proteins and reduced protein solubility, which further increased the number of protein aggregates and changed the structure of the aggregates. Sucrose could be a cryoprotectant and inhibit the influence of freezing on whole egg protein aggregates. Highlights: Aggregate formation upon freezing of the whole egg solution was investigated. It found that the particle number concentration increased during the freezing process. The aggregates became less packed during the freezing process. It was confirmed that the addition of sucrose reduced the degree of structural change of aggregate during freezing. … (more)
- Is Part Of:
- Journal of food engineering. Volume 296(2021)
- Journal:
- Journal of food engineering
- Issue:
- Volume 296(2021)
- Issue Display:
- Volume 296, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 296
- Issue:
- 2021
- Issue Sort Value:
- 2021-0296-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-05
- Subjects:
- Whole egg -- Sucrose -- Freezing process -- Tunable resistive pulse sensing -- Small-angle X-ray scattering
Food industry and trade -- Periodicals
Food -- Analysis -- Periodicals
Aliments -- Industrie et commerce -- Périodiques
Aliments -- Analyse -- Périodiques
Aliments -- Recherche -- Périodiques
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/02608774 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.jfoodeng.2020.110452 ↗
- Languages:
- English
- ISSNs:
- 0260-8774
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4984.543000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 15534.xml