Binding mechanism and structural characteristics of alloyed protein complex for enhanced solubility of hemp seed protein isolate.

Despite the numerous health benefits and high digestibility of hemp seed protein isolate (HPI), its low solubility at neutral pH limits its utilization in the food industry. Therefore, we subjected insoluble HPI and soluble mung bean protein isolate (MBPI) to pH co-shifting under extremely alkaline conditions to form an alloyed protein complex (A-HM). At a mass ratio of HPI:MBPI of 50:50, A-HM exhibited the highest solubility (95.

Effect of Microbial Transglutaminase Treatment on the Techno-Functional Properties of Mung Bean Protein Isolate.

The purpose of this study was to investigate the improvement in techno-functional properties of mung bean protein isolate (MBPI) treated with microbial transglutaminase (MTG), including water- and oil-holding capacity, gelling properties, and emulsifying capacity. MBPI dispersions were incubated with MTG (5 U/g of protein substrate) at 45 °C with constant stirring for 4 h (MTM4) or 8 h (MTM8). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that MTG treatment for different durations increased the amount of high-molecular-weight proteins in MBPI, and most of the cross-linking by MTG was terminated at 8 h.