Some observations on the absorption spectra of various myoglobin derivatives found in meat.

The three principal myoglobin states of haem pigment, oxymyoglobin, metmyoglobin reduced myoglobin, and the ferrous nitrous oxide form, nitrosomyoglobin, were prepared as pure pigments in solution. The absorbance spectra of these solutions were determined and extinction coefficients calculated. The position of the absorption peaks showed some small differences compared to published data, in particular the use of absorbance readings at 525 nm as an isobestic point for all three could be questioned. The use of mathematical transforms to first or second difference functions showed merit for the identification of mixtures of some of the myoglobin forms. The second difference function separated the broad absorbance band in the Soret region into two separate troughs, thereby resolving a mixture of oxymyoglobin and reduced myoglobin. It is suggested that based on absorption spectra, similar mathematical transforms could be applied to the interpretation of reflectance spectra of meat and meat products. Further evaluation of such mathematical transformations is required on a range of meat reflectance spectra.