The effect of heat and transglutaminase treatment on emulsifying and gelling properties of faba bean protein isolate

Abstract The effects of heat treatment (90 °C, 5 or 30 min) and enzymatic crosslinking with transglutaminase (TG, 10, 100 1000 nkat/g protein) on emulsifying gelling properties faba bean protein isolate (FPI) were studied. Heat FPI caused a clear shift in far-UV CD spectra towards random coil structure an increase surface hydrophobicity from 181 to 504 RFU. TG crosslinked heat-treated more efficiently as compared native FPI. TG-induced reduction 435 Emulsifying activity stability indexes stabilized emulsions ranged between 25 30 m2/g 18–35 min, respectively. Rheological the gels induced by heating, followed acidification (10 100 nkat/g analyzed. showed gel-like characteristics at 10% concentration (G? = 180 Pa). When dispersion was further acidified TG-treated (100 nkat/g), G? values >6500 and > 3500 Pa achieved, Water holding capacity >93% >98% for acid- gels, gel microstructures mainly heterogeneously-sized aggregates, however, no differences observed gels.