摘要： The effect of NaNO2 in hydroxyl radical-mediated oxidative damage of yak meat myoglobin was investigated. Laser micro-Raman spectroscopy and Fourier Transform Infrared spectroscopy were used to assess protein (carbonyls, total sulfhydryl and Disulfide bonds) oxidation, atomic (or molecular) interactions and secondary structural changes. The addition of NaNO2 during the oxidation of myoglobin significantly reduced the content of carbonyl and disulfide bonds and protected the sulfhydryl groups from hydroxyl radical oxidation (P < 0.05). There was no significant difference in the secondary structure of myoglobin between the control group and the SN treatment group(P > 0.05). At the same time, NaNO2 had an inhibitory effect on the expansion of the hemoglobin center size and the transition of Fe from a low spin state to a high spin state caused by radical-oxidized. These findings suggest that NaNO2 has potential for treatment effects in a hydroxyl radical-oxidized myoglobin.