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Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins
Author(s) -
Ragucci Sara,
Russo Rosita,
Landi Nicola,
Valletta Mariangela,
Chambery Angela,
Esposito Sabrina,
Raundrup Katrine,
Di Maro Antimo
Publication year - 2019
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.9901
Subject(s) - myoglobin , water buffalo , autoxidation , chemistry , food science , biochemistry , veterinary medicine , medicine
BACKGROUND The Arctic muskox has economic potential as an alternative meat species and is becoming increasingly popular. The present study aimed to determine the primary structure and pseudoperoxidase activity of muskox myoglobin (Mb) compared to cattle and water buffalo myoglobins. RESULTS The primary structure of muskox Mb was determined via a matrix‐assisted laser desorption ionization‐time of flight mass spectrometry‐based mapping approach using the sheep Mb as a reference sequence. The muskox Mb consists of 153 amino acid residues and shows 100% identity with sheep Mb, whereas 98.69% and 97.38% identity is found with cattle and water buffalo Mbs, respectively. Muskox Mb has an autoxidation rate (MetMb formation) higher than both cattle and water buffalo Mbs at pH 7.2 (37 °C). Moreover, its pseudoperoxidase activity is higher than both cattle and water buffalo Mbs at pH 7.4 (physiological pH), whereas it is slightly lower than cattle Mb and higher than water buffalo at a lower pH (5.8), corresponding to the conditions in meat. CONCLUSION For the first time, the present study reports the purification of myoglobin from muskoxen and, furthermore, a comparative study is conducted on autoxidation and pseudoperoxidase activity with respect to cattle and water buffalo Mbs at both physiological and acid pH. Overall, the results of the current research provide novel information for future studies useful to the meat industry when considering the importance of myoglobin as a principal pigment in meat colour stability. © 2019 Society of Chemical Industry