The physicochemical properties of a red pigment in Parma ham were examined in this study and compared with those of other myoglobin (Mb) derivatives whose red color is due to oxymyoglobin (O
2Mb) and nitrosylmyoglobin (NOMb). A water extract of Parma ham was prepared and the absorption spectra of the final filtrate were recorded at 350-650nm. The effects of pH on the absorption spectra were studied subsequent to the addition of NaOH or HCl to the water extract. A single absorption peak was noted at 423nm in the Soret's band and 2 peaks at visible wavelengths of 549 and 587nm. The absorption spectra of red pigment had no change at pH 6-10. At pH 5, the red pigment started to precipitate and increasingly more so as pH became more acidic. No typical absorption peaks for metmyoglobin (MetMb) could be seen at 505 and 630nm at any pH. The sterile water extract of Parma ham was kept in a sterilized test tube for 7 days at low (5°C) or room temperature (20°C) under conditions of light exposure or darkness. The red pigment of the water extract was stable in the dark at each temperature during 7 days of storage. To the water extract of Parma ham and each of the O
2Mb and NOMb solutions, ferricyanide was added. O
2Mb and NOMb were oxidized by ferrycianide to MetMb, but the spectrum of the water extract from Parma ham had no change. The water extract of Parma ham and the O
2Mb and NOMb solutions were heated at 40-70°C for 30min followed by measurement of the absorption spectrum. The heated extract was filtered under sterile conditions. For the water extract, absorption of the spectral peaks decreased, though the spectrum of this pigment was maintained essentially during heating, in contrast to those of O
2Mb and NOMb; precipitation of the pigment was noted with increasing temperature. The pigment precipitated with foreign proteins denatured by heating, but could be detected in its acetone extract.
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