Autoxidation of Beef and Tuna Oxymyoglobins

Autoxidation of Beef and Tuna Oxymyoglobins SUMMARY Rates of autoxidation of beef and tuna oxymyoglobins have been determined at pH 5.9 with various buffer concentrations (0.1, 0.2, and 0.6M) and temperatures ranging from 0 to 40°C. The autoxidation is first‐order with respect to unoxidized myoglobin under all conditions used. The rates of oxidation of tuna oxymyoglobin were independent of buffer concentration, whereas those of beef myoglobin decreased with increasing buffer concentration. Tuna oxymyoglobin was oxidized more slowly than beef at 0 to 10°C at all buffer concentrations, and at higher temperatures and low buffer concentration; at high temperatures and high buffer concentration, tuna oxymyoglobin was oxidized more rapidly than beef. Oxidation of a crude preparation of beef oxymyoglobin was slower than that of purified myoglobin. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

Autoxidation of Beef and Tuna Oxymyoglobins

Journal of Food Science, Volume 28 (2) – Mar 1, 1963

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Publisher
Wiley
Copyright
Copyright © 1963 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
D.O.I.
10.1111/j.1365-2621.1963.tb00185.x
Publisher site
See Article on Publisher Site

Abstract

SUMMARY Rates of autoxidation of beef and tuna oxymyoglobins have been determined at pH 5.9 with various buffer concentrations (0.1, 0.2, and 0.6M) and temperatures ranging from 0 to 40°C. The autoxidation is first‐order with respect to unoxidized myoglobin under all conditions used. The rates of oxidation of tuna oxymyoglobin were independent of buffer concentration, whereas those of beef myoglobin decreased with increasing buffer concentration. Tuna oxymyoglobin was oxidized more slowly than beef at 0 to 10°C at all buffer concentrations, and at higher temperatures and low buffer concentration; at high temperatures and high buffer concentration, tuna oxymyoglobin was oxidized more rapidly than beef. Oxidation of a crude preparation of beef oxymyoglobin was slower than that of purified myoglobin.

Journal

Journal of Food ScienceWiley

Published: Mar 1, 1963

References

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