Improvement of functionality of barley protein by deamidation

• Main Author: Zhao, Jing
• Other Authors: Lingyun Chen, Department of Agricultural, Food and Nutritional Science)
• Format: Others
• Language: en_US
• Published: 2011
• Subjects: Deamidation; barley protein; functionality
• Online Access: http://hdl.handle.net/10048/1837

In this study, the deamidation is involved to modify the structure of barley proteins in terms of prolamin and glutelin in order to improve the functional properties of protein. A wide range of deamidation degrees (0.1% to 45%) were prepared using alkaline method. The results suggested that the optimal deamidation degree of barley prolamin is around 2.4-4.7%, where the solubility, emulsifying and foaming properties of prolamin were significantly improved at both acidic and neutral pHs. The optimal deamidation degree for glutelin is around 2.2 to 5.6%, where deamidated glutelin demonstrated markedly improved solubility at both acidic and neutral pHs. Glutelin performed strong tendency to form aggregates with spherical shape and very large molecular weight. These aggregates are important in stabilizing the emulsions at a broad range of deamidation degree (5.6-43%). These results suggest that barley protein would be an excellent candidate to develop as an emulsifying and foaming ingredient. === Food Science and Technology