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

다국어 초록 (Multilingual Abstract)

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 ofeach type determines the color of the beef. In this study, the influence of denaturing agents and pH on Mbwas examined using fluorescence spectrometers to observe the behavior (folding and unfolding) of Mbas 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, theunfolding decreases with an increase in pH, in accordance with its natural behavior.

참고문헌 (Reference)

1 G. A. Ordway, 207 : 3441-, 2004

2 G. Weber, 27 : 134-, 1959

3 W. J. Bowen, 179 : 235-, 1949

4 S. J. Millar, 42 : 277-, 1996

5 Y. Sugawara, 69 : 583-, 1995

6 E. Gussakovsky, 407 : 120-, 2010

7 K. A. Schenkman, 82 : 86-, 1997

8 S. A. Bylkas, 74 : 426-, 1997

9 H. C. Ferraz, 24 : 101-, 2007

10 C. Mattos, 11 : 761-, 2001

11 C. N. Pace, 131 : 266-, 1986

12 A. N. Schechter, 35 : 567-, 1968

13 J. Torrent, 1764 : 546-, 2006

14 K. A. Dill, 60 : 795-, 1991

15 H. Zhang, 388 : 40-, 2009

16 B. M. Teska, 434 : 153-, 2013

17 J. P. Collman, 104 : 561-, 2004

18 J. M. Glandieres, 227 : 241-, 1995

19 K. C. S. Figueiredo, 28 : 224-, 2009

20 B. Shareghi, "Investigation the activity and stability of lysozyme on presence of magnetic nanoparticles" 한국공업화학회 21 (21): 862-867, 2015