Effect of Heat Treatment for Trypsin Inhibitor Inactivation on Physical and Functional Properties of Peanut Protein

ABSTRACT

Trypsin inhibitor (TI) inactivation in whole peanut kernels exposed to moist heat had a decimal reduction time (D) of 91 min at 100°C and 9.3 min at 120°C. When all processing times were converted to process time at 120°C using Z of 20°C, the composite D at 120°C was 10 min. Solubility decreased with heating to reach a minimum with 98% TI inactivation. Capacities to spontaneously absorb water and to gel were retained better on heating at 120°C than at 100°C for equal TI inactivation. The most functional protein was in kernels heated at 120°C for 10 min. When 20 or 30% meat protein in a meat loaf formulation was replaced with the latter peanut protein, the resulting loaf retained more fat and water and exhibited higher shearing strengths than all meat formulations.