Structuring colloidal oat and faba bean protein particles via enzymatic modification

- Faba bean proteins were intensively crosslinked by transglutaminase.
- Tyrosinase was able to crosslink oat proteins.
- Transglutaminase-treated FPI and OPI showed improved electrostatic stability.
- Foaming properties of oat protein isolate improved upon transglutaminase treatment.
- Transglutaminase improved the colloidal stability of oat protein suspension.

Oat and faba bean protein isolates were treated with transglutaminase from Streptomyces mobaraensis and tyrosinase from Trichoderma reesei to modify the colloidal properties of protein particles in order to improve their colloidal stability and foaming properties. Transglutaminase crosslinked faba bean protein extensively already with 10 nkat/g enzyme dosage. Oat protein was crosslinked to some extent with transglutaminase with higher dosages (100 and 1000 nkat/g). Transglutaminase increased the absolute zeta-potential values and reduced the particle size of oat protein particles. As a result, the colloidal stability and foaming properties were improved. Tyrosinase had limited crosslinking ability on both plant protein materials. Tyrosinase greatly reduced the solubility of oat protein despite limited crosslinking. Tyrosinase did not have effect on zeta-potential or colloidal stability of either protein, but it impaired foaming properties of both. Thus, the crosslinking enzymes studied caused significantly different end product functionality, presumably due to the different mechanism of action.