Influence of pH and temperature on the physicochemical and functional properties of Bambara bean protein isolate

Bambara bean is a rich low-cost protein source and a functional ingredient in the food industry. We investigated the effects of temperature and different pH on the physicochemical and functional properties of Bambara bean protein isolate. Vicilin was the major protein of Bambara bean as revealed by SDS PAGE analysis. The emulsifying capacity of protein isolate was highest at 80 degrees C, pH 9 while emulsion stability was highest at pH 4. Generally, increase in temperature decreased protein solubility at pH 4 and 7, while increase was observed at pH 9 and 100 degrees C. The hydrophobicity of isolate was highest at pH 4 and lowest at pH 9, regardless of temperature. Protein isolate possessed highly compact beta-sheet and alpha-helix secondary structures in proportions greater than 75% (at pH 9 and 50 degrees C). Increase in temperature generally promoted protein rearrangement and partial unfolding. Protein secondary structure and surface hydrophobicity can predict food functionality, directly affecting protein behavior during formulation and long-term storage. This study clearly demonstrated the potential of exploiting pulse protein isolates as nutritional and functional ingredients through temperature and pH control.

Automated summary

The study investigated the effects of temperature and different pH on the physicochemical and functional properties of Bambara bean protein isolate. It found that an increase in temperature generally promoted protein rearrangement and partial unfolding, and that the emulsifying capacity of the protein isolate was highest at 80 degrees C, pH 9 while emulsion stability was highest at pH 4.