TY - JOUR
T1 - Thermal denaturation and autoxidation profiles of carangid fish myoglobins
AU - Hasan, Muhammad Mehedi
AU - Arafah, Purnama
AU - Ozawa, Hideo
AU - Ushio, Hideki
AU - Ochiai, Yoshihiro
N1 - Funding Information:
This work was partly supported by the Japan Society for Promotion of Sciences (KAKENHI # 22380015 to Y. O.).
Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature.
PY - 2021/4
Y1 - 2021/4
N2 - Although myoglobin (Mb) has been considered to be one of the well-characterized proteins, screening of post-genomic era databases revealed the lack of adequate information on teleost Mbs. The present study was aimed to investigate stability and functional features of Mbs from three teleosts of the same family. To unfold how primary structure influences the stability and function of proteins, Mbs were purified from the dark muscles of three carangids, namely, yellowtail, greater amberjack, and silver trevally. Thermostabilities measured by circular dichroism (CD) spectrometry revealed species-specific thermal denaturation pattern, i.e., silver trevally > yellowtail > greater amberjack Mbs. On the other hand, autoxidation rate constants of the ferrous forms of those three carangid Mbs showed positive correlation between the ferrous state of the heme iron and rising temperature. The order of autoxidation rate was in the order of greater amberjack > yellowtail > silver trevally Mbs. The finding of the present study denotes that the thermal stability is not necessarily correlated with the functional stability of carangid Mbs even though their primary structures shared high homology (84–94%).
AB - Although myoglobin (Mb) has been considered to be one of the well-characterized proteins, screening of post-genomic era databases revealed the lack of adequate information on teleost Mbs. The present study was aimed to investigate stability and functional features of Mbs from three teleosts of the same family. To unfold how primary structure influences the stability and function of proteins, Mbs were purified from the dark muscles of three carangids, namely, yellowtail, greater amberjack, and silver trevally. Thermostabilities measured by circular dichroism (CD) spectrometry revealed species-specific thermal denaturation pattern, i.e., silver trevally > yellowtail > greater amberjack Mbs. On the other hand, autoxidation rate constants of the ferrous forms of those three carangid Mbs showed positive correlation between the ferrous state of the heme iron and rising temperature. The order of autoxidation rate was in the order of greater amberjack > yellowtail > silver trevally Mbs. The finding of the present study denotes that the thermal stability is not necessarily correlated with the functional stability of carangid Mbs even though their primary structures shared high homology (84–94%).
KW - Autoxidation
KW - Carangid fish
KW - Myoglobin
KW - Thermostability
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U2 - 10.1007/s10695-021-00928-7
DO - 10.1007/s10695-021-00928-7
M3 - Article
C2 - 33515395
AN - SCOPUS:85099902845
VL - 47
SP - 487
EP - 498
JO - Fish Physiology and Biochemistry
JF - Fish Physiology and Biochemistry
SN - 0920-1742
IS - 2
ER -