Novel interactions of caffeic acid with different hemoglobins: Effects on discoloration and lipid oxidation in different washed muscles
Journal article, 2013
Caffeic acid (CA) accelerated methemoglobin (Hb) formation at pH 5.8 and 25 degrees C. This was attributed to electron donation from CA to liganded O-2 in Hb. CA inhibited hemin dissociation from metHb. Pig Hb remained mostly as oxyHb and did not promote lipid oxidation in washed cod muscle (WCM) nor washed turkey muscle (WTM) during iced storage at pH 5.8. Conversely, perch Hb rapidly was converted to metHb and readily promoted lipid oxidation based on lipid peroxide and hexanal formation. CA strongly inhibited perch Hb-mediated lipid oxidation during storage. Once metHb formation occurred in WCM, CA appeared to maintain the heme protein as metHb during the remainder of iced storage. CA may have become bound to perch Hb based on filtration analysis. CA facilitated the transfer of perch Hb (but not pig Hb) from the aqueous phase to the insoluble components of WCM. Collectively, these results suggest that CA inhibited Hb-mediated lipid oxidation by various mechanisms not related to inhibition of metHb formation
Antioxidants
Myoglobin
Lipid oxidation
metmyoglobin
mediated oxidation
autooxidation
Pigment oxidation
absorption-spectra
fish muscle
Hemoglobin
deoxyhemoglobin
hemin dissociation
autoxidation
oxyhemoglobin
myoglobin
Author
S. Y. Park
University of Wisconsin Madison
Ingrid Undeland
Chalmers, Chemical and Biological Engineering, Life Sciences
T. Sannaveerappa
Limerick Institute of Technology (LIT)
M. P. Richards
University of Wisconsin Madison
Meat Science
0309-1740 (ISSN)
Vol. 95 1 110-117Subject Categories
Food Engineering
DOI
10.1016/j.meatsci.2013.04.003