oxymyoglobin

oxymyoglobin

 [ok″se-mi″o-glo´bin]
myoglobin charged with oxygen.

ox·y·my·o·glo·bin (MbO2),

(ok'sē-mī'ō-glō'bin),
Myoglobin in its oxygenated form, analogous in structure to oxyhemoglobin.

oxymyoglobin

/oxy·myo·glo·bin/ (-mi´o-glo″bin) myoglobin charged with oxygen.

ox·y·my·o·glo·bin

(MbO2) (ok'sē-mī'ŏ-glō'bin)
Myoglobin in its oxygenated form, analogous in structure to oxyhemoglobin.
See also: myoglobin

oxymyoglobin

MbO2; myoglobin charged with oxygen.
References in periodicals archive ?
value in CT and IT treatments, it was primarily because the transformation of bright red oxymyoglobin or light brown metmyoglobin to purplish-red myoglobin was accelerated by the denaturation of the globins or the low oxygen tension during the vacuum marination process (Deman 1999; Lawrie and Ledward 2006), hence the meat color would present darker and redder.
Therefore, changes in the combined concentrations of oxyhaemoglobin and oxymyoglobin in the region of interest (termed, for convenience, [DELTA][Hb[O.
maltaromaticum promotes the formation of oxymyoglobin, most likely through the reduction of ferric compounds to ferrous iron.
This causes a reversion of the bright red oxymyoglobin pigment, which consumers often associated with freshness, to myoglobin--which has a deep purplish red colour.
Adding antioxidants, such as vitamin E, can enhance meat quality and effectively stabilize red oxymyoglobin color by delaying the onset of oxidation.
The colour of meat is determined by the relative amount of three myoglobin derivatives; i) reduced myoglobin, deoxymyoglobin (Mb), which is the purple pigment of deep muscle and known from meat under vacuum, ii) oxygenated myoglobin, oxymyoglobin (MbO2), which is bright cherry red and considered to signify fresh meat by the consumer, and iii) oxidised myoglobin, metmyoglobin (MetMb), which is grey-brown (Rosenvold and Anderson, 2003).
Adding such antioxidants as vitamin E can enhance meat quality and effectively stabilize red, oxymyoglobin color by delaying oxidation.
At low temperatures and low pH values, more oxymyoglobin is formed, leading to increased oxygen solubility and inhibition of oxygen consumption enzyme activity (Kadim et al.
2006) stated that the major function of oxygen is to maintain the myoglobin in its oxymyoglobin state which is cherry cherry-red in color.
Low oxygen concentrations favor oxidation of oxymyoglobin to metmyoglobin; therefore, to minimize metmyoglobin formation in fresh red meat, oxygen must be excluded from the packaging environment to below 0.