Role of lysozyme on liquid egg white foaming properties: Interface behavior, physicochemical characteristics and protein structure. (November 2021)
- Record Type:
- Journal Article
- Title:
- Role of lysozyme on liquid egg white foaming properties: Interface behavior, physicochemical characteristics and protein structure. (November 2021)
- Main Title:
- Role of lysozyme on liquid egg white foaming properties: Interface behavior, physicochemical characteristics and protein structure
- Authors:
- Zhao, Qiannan
Ding, Lixian
Xia, Minquan
Huang, Xi
Isobe, Kazuhiro
Handa, Akihiro
Cai, Zhaoxia - Abstract:
- Abstract: Lysozyme separated from egg white has high economic value and plays an important role in biochemistry, medicine and other fields. The role of lysozyme in the foaming properties of egg white was investigated in this study. After lysozyme being removed, the foaming ability (FA) and the foaming stability (FS) of egg white decreased by 45.1% and 35.3%, respectively, while restored again with lysozyme rejoining. In the absence of lysozyme, the particle size decreased and electrostatic repulsion increased, which resulted in a reduction of the protein adsorption on the interface of foam. Meanwhile, FTIR analysis showed the decrease on the protein secondary structure of α-helix and β-sheet. The reduction of hydrogen bonds played an adverse effect on the formation of stable interface. The decreased viscosity indicated the break of ovomucin-lysozyme complex, which was not conducive to the formation of viscoelastic film and leading to a reduction in FS. Furthermore, in the absence of lysozyme, the high surface tension value of the protein was harmful to the adsorption, stretching and rearrangement of protein molecules on the interface. This research provided a new opinion into the effect of lysozyme on the foaming properties of egg white. Graphical abstract: Image 1 Highlights: The foaming properties of egg white become worse with the elimination of lysozyme. In the absence of lysozyme, the egg white foam becomes larger and sparser. Electrostatic interaction mainly accountsAbstract: Lysozyme separated from egg white has high economic value and plays an important role in biochemistry, medicine and other fields. The role of lysozyme in the foaming properties of egg white was investigated in this study. After lysozyme being removed, the foaming ability (FA) and the foaming stability (FS) of egg white decreased by 45.1% and 35.3%, respectively, while restored again with lysozyme rejoining. In the absence of lysozyme, the particle size decreased and electrostatic repulsion increased, which resulted in a reduction of the protein adsorption on the interface of foam. Meanwhile, FTIR analysis showed the decrease on the protein secondary structure of α-helix and β-sheet. The reduction of hydrogen bonds played an adverse effect on the formation of stable interface. The decreased viscosity indicated the break of ovomucin-lysozyme complex, which was not conducive to the formation of viscoelastic film and leading to a reduction in FS. Furthermore, in the absence of lysozyme, the high surface tension value of the protein was harmful to the adsorption, stretching and rearrangement of protein molecules on the interface. This research provided a new opinion into the effect of lysozyme on the foaming properties of egg white. Graphical abstract: Image 1 Highlights: The foaming properties of egg white become worse with the elimination of lysozyme. In the absence of lysozyme, the egg white foam becomes larger and sparser. Electrostatic interaction mainly accounts for the impacts of lysozyme on the foaming. The poor foam stability is due to the destruction of the lysozyme-ovomucin complex. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 120(2021)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 120(2021)
- Issue Display:
- Volume 120, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 120
- Issue:
- 2021
- Issue Sort Value:
- 2021-0120-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-11
- Subjects:
- Foaming ability -- Foaming stability -- Egg white -- Lysozyme -- Protein interaction
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2021.106876 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 17535.xml