Investigating the physicochemical properties and air-water interface adsorption behavior of transglutaminase-crosslinking rapeseed protein isolate.

Improving the technical functionality to adapt to the application of complex food systems is an important challenge for the development of plant protein ingredients. Herein, the correlation between the physicochemical properties and interfacial adsorption behavior of rapeseed protein isolate (RPI) at the air-water interface after transglutaminase (TG) treatment was investigated. The results of cross-linking degree, Fourier transform infrared spectroscopy (FTIR) and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that the TG enzyme was able to catalyse cross-linking between lysine and glutamine residues of RPI. The foaming capacity of RPI was enhanced from 120 % to 150 % after TG cross-linking 5 h, whereas the average size (210-219 nm) of the RPI determined by dynamic light scattering did not change significantly. Besides, the hydrophobicity tended to increase overall under the enzyme treatment, while the surface electrostatic potential decreased. The former indicates the unfolding of the protein and reduces the kinetic barriers to protein adsorption at the air-water interface, with a consequent increase in disulfide bonding and surface pressure. Furthermore, as the enzyme treatment time increased, a significant increase in protein content of foam by 33.86 %. These findings provide novel insight into the foaming mechanism of TG cross-linking RPI.