Spectroscopic characterization of biochemical states of myoglobin in beef in different environments

Jae-Kwang Kim; Eun Kyoung Song; Tae Joo Park; Chang-Joon Kim

Journal of Industrial and Engineering Chemistry, Vol.28, 302-306, August, 2015

DOI10.1016/j.jiec.2015.03.007 Export Citation

Spectroscopic characterization of biochemical states of myoglobin in beef in different environments

Jae-Kwang Kim, Eun Kyoung Song¹, Tae Joo Park^{1, †}, and Chang-Joon Kim^{2, †}

School of Energy & Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan 689-798, Republic of Korea
¹School of Life Science, Ulsan National Institute of Science and Technology (UNIST), Ulsan 689-798, Republic of Korea
²Department of Chemical Engineering & ERI, Gyeongsang National University, 501 Jinju-daero, Jinju, Gyeongnam 660-701, Republic of Korea

E-mail:,

The two states of myoglobin (Mb) in beef were firstly investigated using a spectrophotometer. Oxymyoglobin (Oxy-Mb) and metmyoglobin (Met-Mb) coexist in the primary beef, where the amount of each type determines the color of the beef. In this study, the influence of denaturing agents and pH on Mb was examined using fluorescence spectrometers to observe the behavior (folding and unfolding) of Mb as a function of different concentrations of denaturing agents (GuHCl and Urea) and different pH values. The unfolding of Mb is increased with an increasing concentration of denaturing agents. However, the unfolding decreases with an increase in pH, in accordance with its natural behavior.

Keywords:Myoglobin;Absorption spectroscopy;Fluorescence spectroscopy;Biochemistry

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Teska BM, Li C, Winn BC, Arthur KK, Jiang Y, Gabrielson JP, Anal. Biochem., 434, 153 (2013)
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Figueiredo KCS, Ferraz HC, Borges CP, Alves TLM, Protein J., 28, 224 (2009)
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[1] Ordway GA, Garry DJ, J. Environ. Biol., 207, 3441 (2004)

[2] Bylkas SA, Andersson LA, J. Chem. Educ., 74, 426 (1997)

[3] Bowen WJ, J. Biol. Chem., 179, 235 (1949)

[4] Millar SJ, Moss BW, Stevenson MH, Meat Sci., 42, 277 (1996)

[5] Sugawara Y, Matsuoka A, Kaino A, Shikama K, Biophys. J., 69, 583 (1995)

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[9] Ferraz HC, Duarte LT, Di LM, Alves TLM, Habert AC, Borges CP, Braz. J. Chem. Eng., 24, 101 (2007)

[10] Mattos C, Ringe D, Curr. Opin. Struct. Biol., 11, 761 (2001)

[11] Pace CN, Methods Enzymol., 131, 266 (1986)

[12] Schechter AN, Epstein CJ, J. Mol. Biol., 35, 567 (1968)

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[14] Dill KA, Shortle D, Annu. Rev. Biochem., 60, 795 (1991)

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