Characterisation and application of bambara protein-polysaccharide complex coacervates in encapsulation of bioactive compounds

Abstract

Bambara groundnut (Vigna subterranea) is a leguminous crop that is indigenous to Africa. In South Africa, the legume is cultivated in KZN, Limpopo and Mpumalanga where it is considered a traditional food. Bambara groundnut is a good source of protein (15 – 28 %) and contains substantial amounts of starch. The legume thrives well in areas of low agricultural input. Despite its good protein content, bambara groundnut is mostly cultivated in rural areas for by subsistence farmers. In recent years, there has been increased interest in bambara groundnut protein as an alternative protein source. The purpose of this study is to investigate the complexation behavior of bambara protein with gum Arabic and test the application of the formed complexes in encapsulation and delivery of bioactive compounds. In the first part of this study, four protein fractions extracted at different pH including the salt-solubilisation method were complexed with gum Arabic. The protein content as well as physicochemical properties (SDS-PAGE, FTIR, Zeta potential, SEM) of the protein fractions and resulting bambara protein-gum Arabic (BPI-GA) complexes were then investigated. In subsequent parts of the study, bambara protein extracted by the salt-solubilisation method was complexed with gum Arabic. The influence of ionic strength and biopolymer mixing ratio on complex formation was investigated. Subsequently, the emulsification properties, foaming properties, encapsulation efficiency and release properties of the formed complexes were also investigated under simulated gastric and intestinal pH conditions. The salt-soluble fraction showed the highest protein content (82%) whilst the lowest protein content (76%) was recorded at pH 2. The FTIR analyses revealed an increase in β-sheet content with decrease in pH of extraction. Complexation of the protein fractions with GA resulted in the optimal pHs of interaction shifting towards acidic regions (pHopt: 4.8 to 2.9) as pH of protein extraction became more acidic. Upon complexation, protein fractions produced coacervate yields ranging between 41 - 68%, with the pH 2 fraction recording the lowest (41%) yield. Further, addition of gum arabic seemed to broaden the turbidity profiles. When assessed by SEM, the particles appeared as spherical and aggregated structures between 100-200 nm.