Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme.

Dynamic and steady shear rheology is used to examine the synthesis of low-pH (approximately 4) whey protein gels obtained through a two-step process. The first step involves cross-linking of whey proteins at pH 8 and 50 degrees C using transglutaminase enzyme, while the second step entails cold-set acidification of the resulting solution using glucono-delta-lactone (GDL) acid. During the first step, the sample undergoes enzyme-catalyzed epsilon-(gamma-glutamyl)lysine bond formation with a substantial increase in viscosity. Acidification in the second step using GDL acid leads to a rapid decrease in pH with a concomitant increase in the elastic (G') and viscous (G' ') moduli and formation of a gelled network. We examine the large strain behavior of the gel samples using a relatively new approach that entails plotting the product of elastic modulus and strain (G'gamma) as a function of increasing dynamic strain and looking for a maximum, which corresponds to the yield or fracture point. We find the enzyme-catalyzed gels to have significantly higher yield/fracture stress and strain compared to cold-set gels prepared without enzyme or conventional heat-set gels. In addition, the elastic modulus of the enzyme-catalyzed gel is also higher than its non-enzyme-treated counterpart. These results are discussed in terms of the gel microstructure and the role played by the enzyme-induced cross-links.