Proteomic profile of broccoli flower proteins for potential applications in the food industry
Fidele Benimana, Nancy Alila, Kentaro Kawata, Anupam Singha Roy, Christopher Kucha, Anand Mohan
Abstract
Growing demands for plant proteins are driven by the great potential of this protein source to improve food functionality, nutritional value, and environmental sustainability. This research characterized functional, thermal, and structural properties and protein profile (Brassica oleracea var. italica) flower. The various protein fractions were extracted using Osborne's sequential extraction, giving 89.60% of crude protein. Among the yields, glutelin had the highest value, at 12.75 ± 1.07 g; this was followed by albumin, 4.75 ± 0.53 g; globulin, 1.05 ± 0.48 g; and prolamin, 0.42 ± 0.06 g. Antioxidant activity assay showed higher activity for albumin and higher total phenolic content for prolamin. Sodium Dodecyl Sulfate gel electrophoresis yielded various profiles, and through Differential Scanning Calorimetry analysis, glutelin was proved to be more thermally stable (peak denaturation temperature of 82.50 ± 0.05 °C). Functional properties were also determined: glutelin had the highest foaming and water-holding capacity; albumin had the highest oil-holding capacity. Albumin and glutelin demonstrated high emulsifying activity. Proteomic analysis identified 1681 proteins, globulins (45%) and albumins (29%). Results show that broccoli flower proteins could have great potential for improving food attributes, extending shelf life, and being used as natural food additives. • Plant-derived proteins have the potential to improve food functionality and nutritional value. • The functional, thermal, and structural properties of Broccoli flower proteins were characterized. • Among the yields, glutelin had the highest value, followed by albumin, globulin, and prolamin. • Broccoli edible flower proteins are natural food ingredients with functional, thermal, and structural benefits.