The role of peracetic acid in bloodmeal decoloring

Abstract

Hydrogen peroxide (HP) can degrade soluble heme, forming yellow or colorless degradation products. Thermal treatment during bloodmeal production changes the conformation of oxyhemoglobin trapping heme in hydrophobic protein regions or forms methemoglobin (metHb) heme which catalytically removes HP. As a result, HP can only degrade a portion of the heme present in bloodmeal leading to poor decoloring. Equilibrium peracetic acid (PAA) solutions can effectively decolor bloodmeal. This work assessed the ability of PAA to decolor bloodmeal and the mechanism by which it occurs. The inability of HP to decolor bloodmeal is determined by the fact that it is unable to permanently degrade metHb heme, or hydrophobically trapped heme. Addition of organic acids to HP led to significant swelling of the protein chains but also to poorer decoloring and lower HP consumption compared to PAA. This suggested that in the case of PAA solutions, where bleaching was facile, the reason PAA solutions are capable of decoloring bloodmeal was due to the action of the PAA molecule against heme, whereas HP and acetic (ethanoic) acid played only minor roles in total bleaching. The decolored protein powder has reduced odor and whiter color, and is suitable for applications such as bioplastics.