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Novel interactions of caffeic acid with different hemoglobins: Effects on discoloration and lipid oxidation in different washed muscles

S. Y. Park ; Ingrid Undeland (Institutionen för kemi- och bioteknik, Livsmedelsvetenskap) ; T. Sannaveerappa ; M. P. Richards
Meat Science (0309-1740). Vol. 95 (2013), 1, p. 110-117.
[Artikel, refereegranskad vetenskaplig]

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

Nyckelord: Antioxidants, Hemoglobin, Myoglobin, Lipid oxidation, Pigment oxidation, hemin dissociation, fish muscle, mediated oxidation, absorption-spectra, myoglobin, deoxyhemoglobin, autooxidation, oxyhemoglobin, metmyoglobin, autoxidation

Denna post skapades 2013-07-29.
CPL Pubid: 180285


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Institutionen för kemi- och bioteknik, Livsmedelsvetenskap (2005-2014)



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