The effect of transglutaminase crosslinking on the rheological characteristics of heated peanut flour dispersions.

Peanut flour (PF) is a high-protein ingredient prepared after the partial extraction of oil from roasted peanut seed. Microbial transglutaminase (TGase) catalyzes protein crosslinking via acyl-transfer reactions, resulting in the modification of functional properties such as viscosity, gelation, solubility, and water holding capacity. This work was conducted to observe changes in rheological properties of PF dispersions in the presence and the absence of TGase and amidated pectin (AP). Dispersions were characterized across a range of conditions, including controlled heating and cooling rates under both large- and small-strain deformations. Gelation occurred at temperatures above 78 degrees C using PF dispersions treated with TGase compared to untreated dispersions devoid of the enzyme (about 68 degrees C). The addition of AP (0.5%) resulted in a general increase in viscoelasticity for all dispersions. AP addition also minimized the shift in gel point temperature caused by TGase polymerization reactions. High-molecular-weight polymers were formed in TGase-treated PF dispersions in both the presence and the absence of AP; however, polymer formation was more rapid in PF dispersions without AP. Ortho-phthaldialdehyde assays indicated about 40% protein coupling in PF dispersions treated with TGase compared to about 20% in those containing both AP and TGase. Collectively, these data suggest potential applications of TGase-treated PF dispersions, both in the presence and the absence of AP, for use in peanut-base food products, including protein bars, shakes, and value-added baked goods.