Premium
Effect of Heat Treatment for Trypsin Inhibitor Inactivation on Physical and Functional Properties of Peanut Protein
Author(s) -
PERKINS D.,
TOLEDO R. T.
Publication year - 1982
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1982.tb12745.x
Subject(s) - chemistry , trypsin , trypsin inhibitor , food science , solubility , chromatography , biochemistry , enzyme , organic chemistry
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.