1. In oxidized meat, the meat loses oxygen and is oxidized to Fe3+. According to the data, after the oxidizing agent (K6[FeCN6]) was added, the absorption of oxidized metmyoglobin was recorded as 0.76 which is higher than oxy-Myoglobin 0.120. What does this indicates???? what does it means?????2.However, when reducing reagent was added, the absorption of oxymyoglobin is 0.783 which is higher than 0.100 of metmyoglobin.Why is this significant?3.can this data help to indicates that oxymyoglobin preferred bright red color. Metmyoglobin prefered brown color, and is more susceptible than oxymyoglobin to oxidation? Met-Myoglobin (Fe3+)OriginalOxidized Sample Fe3+Reduced Sample Fe2+0.100Beer-Lambert Law A = Ecl A = absorbance (no units).0.2700.760Oxy-Myoglobin (Fe2+)0.4000.1200.783 Absorbance (OD)0.50.40.3-0.20.1metmyoglobin500520540oxymyoglobin560 580deoxymyoglobin600 620Wavelength (nm)I640660680 7001,2Myoglobin is easily extracted from a lean ground steak patty. The meatcontains very high levels of both Oxy-Mb and Met-Mb, which have unique spectralproperties. Table I illustrates the wavelengths of maximum absorbance peaks. Theunique spectral properties can be used to accurately identify and characterize the sampleidentity with respect to both oxidation state and functional state.

Myoglobin (Mb) is an iron and oxygen binding protein found in the cardiac and skeleton muscles of vertebrates and also in all mammals. Mb has higher affinity for oxygen and doesn't shows cooperative binding like Hemoglobin (Hb). Thus, Mb can hold the oxygen for longer during and more tightly. In human, Mb is found only during muscle injury. Mb functions as - oxygen transport to muscle, storage of oxygen and also scavenger of reactive oxygen species. Mb is globin cytoplasmic single chain protein which binds to oxygen at its Heme group. It is contains porphyrin ring with iron in its center. Binding of oxygen causes significant structural change in Fe center, ultimately reduces the radius and moves towards the center of pocket. Oxy-Mb is oxygenated Mb, which its main function i.e. storage of oxygen with oxidation state of Fe2+. it gives bright red color to meat, mostly in living tissue. Deoxy-Mb is deoxygenated Mb, when Mb is deoxygenated and gives purple-red color. Deoxy-Mb oxidation state is Fe2+ . Met-Mb is is the oxidized form of Mb. It causes typical coloration in the meat. Met-Mb oxidation state id Fe3+. Both oxy-Mb and deoxy-Mb are normal Mb present in the living muscles. Oxidation of Oxy-Mb and deoxy-Mb gives Met-Mb. 1. In oxidized meat, the meat loses oxygen and is oxidized to Fe3+. According to the data, after the addition of oxidizing agent (K6[FeCN6]), the absorption maxima of oxidized metmyoglobin was observed as 0.76. It is higher than oxy-Myoglobin 0.120. It indicates that the oxy-Mb is more capable to oxidation due to the presence of oxidizing agent (K6[FeCN6]) and oxy-Mb oxidized into Met-Mb. While, Met-Mb is not susceptible to oxidation as it is an oxidizing agent. So, oxy-Mb (Fe+2) is oxidized (loss of electrons) into Met-Mb (Fe+3) in presence of oxidizing agent K6[FeCN6. Therefore, overall absorbance value of Met-Mb is more as compared to oxy-Mb. 2. However, when reducing reagent was added, the absorption of oxymyoglobin is 0.783 which is higher than 0.100 of metmyoglobin. In presence of reducing agent, Met-Mb (Fe+3) is reduced into oxy-Mb (F+2) i.e. gain of electrons (reduction). Thus, it increases the overall absorbance value of oxy-Mb than the Met-Mb. 3. Yes, the given data indicates that oxymyoglobin is preferred to be bright red color. Because the absorbance of Oxy-Mb in original sample is 0.4 which is more than the met-Mb (0.27). We know that the reduced form of Mb gives bright red color (oxy-Mb, Fe+2) while the oxidized form of Mb gives brown color (Met-Mb, Fe+3). Yes, Met-Mb is more susceptible than oxymyoglobin to oxidation. Met-Mb concentration in living muscles is very small due to enzyme met-myoglobin reductase which converts prosthetic group Fe3+ into Fe2+ (normal Mb) in the presence of NADH. Met-Mb reduction limits the oxidation of Mb i.e. Met-Mb works by the gain of electrons to limit the loss of electrons. Thus, Met-Mb is more capable to oxidation as compared to oxy-Mb.