Because of the presence of proteinase inhibitors the enzymatic modification of egg-white protein demands a heating process to inactivate the inhibitors before enzyme action. The herewith occuring strong coagulation of the protein complicates the course of enzymatic hydrolysis. A laboratory process i
Modification of functional properties of egg-white proteins
✍ Scribed by Campbell, Lydia ;Raikos, Vassilios ;Euston, Stephen R.
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 674 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0027-769X
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✦ Synopsis
Abstract
Egg‐white proteins are extensively utilised as food ingredients due to their unique functional properties. Several attempts have been made in order to improve the functional properties of egg‐white proteins and to identify the optimal formulations for unique food products. Experimental data proves that controlled denaturation of egg‐white proteins can have a beneficial impact on various functional applications in the food industry such as emulsifying ability, heat stability, gelation. This review describes the effect of heat‐induced denaturation on protein structure and functionality. Studies on the impact of Maillard reaction, which aim to elucidate the structure‐function relationship of egg‐white proteins, are presented. A novel approach which could be the basis for the development of new methods aiming to improve the functional properties of egg‐white proteins is also discussed.
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