Spectroscopic characterization of biochemical states of myoglobin in beef in different environments

Abstract

The two states of myoglobin (Mb) in beef were firstly investigated using a spectrophotometer. Oxymyoglobin (Oxy-Mb) and metmyoglobin (Met-Mb) coexist in the primary beef, where the amount of each type determines the color of the beef. In this study, the influence of denaturing agents and pH on Mb was examined using fluorescence spectrometers to observe the behavior (folding and unfolding) of Mb as a function of different concentrations of denaturing agents (GuHCl and Urea) and different pH values. The unfolding of Mb is increased with an increasing concentration of denaturing agents. However, the unfolding decreases with an increase in pH, in accordance with its natural behavior.