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

Outi Nivala*, Emilia Nordlund, Kristiina Kruus, Dilek Ercili-Cura

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

Abstract

The effects of heat treatment (90 °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 – 30 m2/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.
Original languageEnglish
Article number110517
JournalLWT: FOOD SCIENCE AND TECHNOLOGY
DOIs
Publication statusE-pub ahead of print - 6 Nov 2020
MoE publication typeA1 Journal article-refereed

Keywords

  • Emulsification
  • Faba bean
  • Gelation
  • Surface hydrophobicity
  • Transglutaminase

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