首页|The effect of heat and transglutaminase treatment on emulsifying and gelling properties of faba bean protein isolate
The effect of heat and transglutaminase treatment on emulsifying and gelling properties of faba bean protein isolate
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NSTL
Elsevier
The effects of heat treatment (90 degrees C, 5 or 30 min) and enzymatic crosslinking with transglutaminase (TG, 10, 100 or 1000 nkat/g protein) on emulsifying and gelling properties of faba bean protein isolate (FPI) were studied. Heat treatment of FPI caused a clear shift in far-UV CD spectra towards random coil structure and an increase in surface hydrophobicity from 181 to 504 RFU. TG crosslinked heat-treated FPI more efficiently as compared to native FPI. TG-induced crosslinking caused a reduction of surface hydrophobicity from 504 to 435 RFU. Emulsifying activity and stability indexes of FPI stabilized emulsions ranged between 25 and 30 m(2)/g and 18-35 min, respectively. Rheological properties of the FPI gels induced by heating, followed by acidification or TG treatment (10 or 100 nkat/g protein) were analyzed. FPI showed gel-like characteristics at 10% concentration (G' = 180 Pa). When the heat-treated FPI dispersion was further acidified or TG-treated (100 nkat/g), G' values of >6500 and > 3500 Pa were achieved, respectively. Water holding capacity of the FPI gels were >93% and >98% for acid- and TG-induced gels, respectively. The gel microstructures showed mainly heterogeneously-sized protein aggregates, however, no differences were observed between acid- and TG-induced gels.
NSTL
Elsevier
