Mass spectrometric characterization and redox instability of turkey and chicken myoglobins as induced by unsaturated aldehydes.
Turkey and chicken myoglobins (Mbs) were isolated, purified, and characterized using electrospray ionization mass spectrometry (ESI-MS), and the effect of unsaturated aldehydes (nonenal and hexenal) on their redox stability was investigated in vitro. The deconvoluted spectra from ESI-MS exhibited a molecular mass of 17291 Da for both turkey and chicken Mbs. Significant homogeneity in the fragmentation pattern of both Mbs was indicated by ESI-MS/MS. Both turkey and chicken oxymyoglobins (OxyMbs) were more prone to oxidation at pH 5.8 than at pH 7.4. Metmyoglobin formation was greater in the presence of unsaturated aldehydes than controls (P < 0.05). The results demonstrated that both turkey and chicken Mbs have identical molecular mass and that the effects of alpha,beta-unsaturated aldehydes on their redox stability are consistent with those of mammalian livestock Mbs.
Maheswarappa
Naveena B
NB
National Research Centre on Meat, Chengicherla Hyderabad, Andhra Pradesh 500039, India.
Faustman
Cameron
C
Tatiyaborworntham
Nantawat
N
Yin
Shuang
S
Ramanathan
Ranjith
R
Mancini
Richard A
RA
D000447:Aldehydes / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D002645:Chickens; D004355:Drug Stability; D008786:Metmyoglobin / Q000737:chemistry; D009132:Muscles / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry* / Q000302:isolation & purification; D010084:Oxidation-Reduction; D021241:Spectrometry, Mass, Electrospray Ionization; D014422:Turkeys
D000447:Aldehydes; D009211:Myoglobin; D008786:Metmyoglobin; C027576:4-hydroxy-2-nonenal