Structure, composition and functional properties of storage proteins extracted from bambara groundnut (Vigna subterranea) landraces. (27th February 2017)

• Record Type: Journal Article
• Authors: Arise, Abimbola K.; Nwachukwu, Ifeanyi D.; Aluko, Rotimi E.; Amonsou, Eric O.
• Is Part Of: International journal of food science & technology. Volume 52:Number 5(2017)
• Page Start: 1211
• Page End: 1220
• Publication Date: 2017-02-27
• Subjects: Bambara groundnut -- circular dichroism -- landrace -- protein isolate -- solubility -- thermal properties; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.13386
• Languages: English
• ISSNs: 0950-5423

Abstract

Abstract: Bambara groundnut is a protein‐rich traditional legume. In this study, storage proteins were isolated from three bambara landraces. Bambara protein revealed four major protein bands: one broad band at 55 kDa, two medium bands at 62 kDa and 80 kDa and a high molecular weight (HMW) protein at 141 kDa. The vicilin (7S) subunits with molecular weight of 55 kDa and 62 kDa were major fractions in bambara storage proteins. Bambara proteins showed two endothermic peaks ranging from 64 to 69 °C and 76 to 90 °C, respectively. Bambara protein isolates had well‐defined tertiary and secondary structures, respectively, at pH 3.0, and this well‐defined structure decreased slightly at higher pH values. The isolates revealed a strong secondary structure dominated by α‐helical conformation. Foaming capacities of bambara proteins were dependent on pH with maximum percentage FC observed at pH 3.0, while the emulsion activity increased with increasing pH for all the isolates. Vicilin (7S) fraction seems to be the major storage protein fraction of bambara. Bambara proteins could serve as excellent ingredients for the formulation of food foams and emulsions. Abstract : Storage proteins were extracted from Bambara landraces and characterised. The vicilin (7S) subunits were major fractions of bambara protein. The isolates revealed a strong secondary structure dominated mostly by α‐helix conformation. Bambara storage proteins are thermally stable and display good foaming and emulsion activities.