Protein network formation during pound cake making: The role of egg white proteins and wheat flour gliadins. (December 2016)
- Record Type:
- Journal Article
- Title:
- Protein network formation during pound cake making: The role of egg white proteins and wheat flour gliadins. (December 2016)
- Main Title:
- Protein network formation during pound cake making: The role of egg white proteins and wheat flour gliadins
- Authors:
- Deleu, Lomme J.
Wilderjans, Edith
Van Haesendonck, Ingrid
Brijs, Kristof
Delcour, Jan A. - Abstract:
- Abstract: During pound cake baking, structure sets as a result of starch gelatinization and protein network formation. These processes are crucial for pound cake quality. However, the relative contribution of the different proteins to the network formation has hardly been studied. Here, protein extraction in different media and size-exclusion HPLC analysis are used to monitor 15 N-labeled egg white protein and gliadin involvement in the protein network formation during cake making. Thermal denaturation of the different egg white proteins codetermines their incorporation in the network. Ovotransferrin, ovomucoid and lysozyme are the first to be incorporated in the network. In the process, sulfhydryl/disulfide exchange reactions with other proteins play a key role. In a later phase, ovalbumin is also incorporated. The latter has free sulfhydryl groups and further reacts with α- and γ-gliadins by sulfhydryl/disulfide exchange reactions. Our work demonstrates for the first time a mixed network in cake which contains protein from both egg white and wheat flour. The ω-gliadins lack both sulfhydryl groups and disulfide bonds and are not incorporated in the protein network. Graphical abstract: Highlights: Egg white and wheat flour proteins take part in the same covalent network. Ovalbumin determines the incorporation of α- and γ-gliadin. Other egg white proteins form disulfide bonds with proteins from other ingredients. ω-Gliadin is not incorporated in the covalent protein networkAbstract: During pound cake baking, structure sets as a result of starch gelatinization and protein network formation. These processes are crucial for pound cake quality. However, the relative contribution of the different proteins to the network formation has hardly been studied. Here, protein extraction in different media and size-exclusion HPLC analysis are used to monitor 15 N-labeled egg white protein and gliadin involvement in the protein network formation during cake making. Thermal denaturation of the different egg white proteins codetermines their incorporation in the network. Ovotransferrin, ovomucoid and lysozyme are the first to be incorporated in the network. In the process, sulfhydryl/disulfide exchange reactions with other proteins play a key role. In a later phase, ovalbumin is also incorporated. The latter has free sulfhydryl groups and further reacts with α- and γ-gliadins by sulfhydryl/disulfide exchange reactions. Our work demonstrates for the first time a mixed network in cake which contains protein from both egg white and wheat flour. The ω-gliadins lack both sulfhydryl groups and disulfide bonds and are not incorporated in the protein network. Graphical abstract: Highlights: Egg white and wheat flour proteins take part in the same covalent network. Ovalbumin determines the incorporation of α- and γ-gliadin. Other egg white proteins form disulfide bonds with proteins from other ingredients. ω-Gliadin is not incorporated in the covalent protein network in pound cake. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 61(2016:Dec.)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 61(2016:Dec.)
- Issue Display:
- Volume 61 (2016)
- Year:
- 2016
- Volume:
- 61
- Issue Sort Value:
- 2016-0061-0000-0000
- Page Start:
- 409
- Page End:
- 414
- Publication Date:
- 2016-12
- Subjects:
- Mixed protein network -- Pound cake -- Ovalbumin -- Gliadin
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.2016.05.001 ↗
- 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:
- 7472.xml