Preparation and characterization of protein isolate from fresh and hardened beans (Phaseolus vulgaris L.).

The purpose of the present work was to determine the effect of accelerated hardening of beans on yield and physicochemical, functional, and toxicological properties. Protein isolates were obtained from fresh and hardened common beans (Phaseolusvulgaris L.). Acid treatment was an effective method to produce hardened bean. Protein recovery in the isolation procedure for fresh bean isolate (FBI) was 45.5% and 36.15% for hardened bean isolate (HBI); however, the amount of protein was similar in both isolates. In general, the amino acid pattern was similar in both isolates. Electrophoresis analysis showed that the main protein (phaseolin) remained unchanged during the isolation procedure. HBI showed a decrease in the bands of 14 to 26 kDa corresponding to the phytohemagglutinin group, and this was associated with a 56.6% decrease in the concentration of the trypsin inhibitor (TI). Heat treatment of FBI reduced 89.4% of the TI and the hemagglutining activities, and it was reflected in an adequate weight gain of young animals. FBI showed better functional properties than HBI, and both isolates showed the same amount of flavonoids.