Physicochemical characteristics and <scp>pH</scp> ‐dependent functional properties of the coconut meal protein fractions

BACKGROUND: Coconut meal protein is considered a promising source of protein, however its utilization is highly dependent on physicochemical characteristics and functional properties. Albumin, globulin, glutelin, and gliadin were obtained from coconut meal protein via isoelectric precipitation, and their physicochemical and pH-dependent functional properties were analyzed. RESULTS: The results of gel electrophoresis showed that molecular weight of albumin, globulin, and gliadin ranged from < 75 kDa. Glutelin showed darker staining on the lanes and may have a relatively large molecular weight. Among the coconut meal protein fractions, globulin showed the most prominent conformational unfolding, superior thermal stability, and a higher number of sulfhydryl groups and disulfide bonds. Additionally, the coconut meal protein fractions exhibited optimal functional properties at pH 9.0, followed by pH 7.0 and pH 3.0. Furthermore, albumin and globulin demonstrated better water/oil holding capacities, foaming properties, and solubility. In particular, globulin displayed significantly higher emulsification capacity compared to other protein fractions, similar to the emulsification properties of soybean isolate protein. CONCLUSION: Overall, the excellent functional properties of globulin showed promising novel plant proteins that can be used as an effective food ingredient to improve product diversification. © 2026 Society of Chemical Industry.