Myoglobin content and oxidative status to understand meat products’ color: Phenomenological based model

Abstract

Meat color is attributed to myoglobin concentration and redox state. Myoglobin is a water-soluble hemoprotein with iron in its prosthetic group, which defines myoglobin’s redox state via its valence state and ligand linked to the free coordination site. In fresh meat, myoglobin can be in one of three states in dynamic equilibrium: deoxymyoglobin, oxymyoglobin, and metmyoglobin. Myoglobin can chemically interact with numerous components in meat products, affecting its redox state. These structural alterations in myoglobin caused by processing conditions will affect its thermal stability and consequently meat product color. Presently, cured meat products are made with sodium nitrite, a curing agent that reacts with myoglobin in meat, forming nitrosomyoglobin, a stable compound that gives the final meat product a distinctive pink color. This work proposes a mathematical model for understanding myoglobin structural changes during the production of a cured meat product. Because of the phenomenological structure of the established model, valuable knowledge is obtained, allowing new possibilities to be explored in the color of meat products while considering the chemical state of myoglobin. The proposed phenomenological model is validated with an error of roughly 10%.