5 research outputs found
Traditional halal meat production without stunning versus commercial slaughter with electrical stunning of slow-growing broiler chicken: impact on meat quality and proteome changes
ABSTRACT: Impact of traditional halal meat production without stunning (NST) and commercial slaughter with electrical stunning (ST) of 100 slow-growing broiler chicken on blood plasma and different biochemical, enzymatic, hormonal, meat quality, and proteomic changes was evaluated. The results revealed lower (P 0.05) in blood glucose, lactate dehydrogenase (LDH), creatine kinase (CK), thyroxine (T4), cortisol, and aspartate aminotransferase (AST) was observed relative to NST samples. The 2-dimensional gel electrophoresis (2-DE) coupled to MALDI-TOF MS of meat samples has identified 14 differentially abundant proteins between 2 groups. Proteins demonstrating positive correlation with stress namely adenylate kinase isoenzyme-1, Rho guanine nucleotide exchange factor (NST), and apolipoprotein A-I (ST) were overabundant. From the current study, it is concluded that electrical stunning of broilers prior to slaughter or traditional halal slaughter without stunning does not adversely affect the meat quality
Redox Instability and Hemin Loss of Mutant Sperm Whale Myoglobins Induced by 4‑Hydroxynonenal in Vitro
The effects of 4-hydroxy-2-nonenal (HNE) on redox stability
of
Oxy- and Deoxy- wild-type (WT) and recombinant sperm whale myoglobins
(P88H/Q152H, L29F, H97A, and H64F) and hemin loss from Met-myoglobin
(Mb) were investigated. HNE induced greater redox instability in WT
and mutant Mbs compared to controls (<i>p</i> < 0.05).
The extent of HNE-induced OxyMb oxidation was lesser in L29F (<i>p</i> < 0.05) and greater in H97A and P88H/Q152H than in
WT (<i>p</i> < 0.05). H64F DeoxyMb was more redox stable
than WT DeoxyMb in the presence of HNE (<i>p</i> < 0.05).
HNE alkylation occurred exclusively on histidine residues, and histidine
48 was alkylated in all sperm whale myoglobins. HNE alkylation accelerated
the protoporphyrin moiety loss only in H97A. Met- forms of WT and
L29F but not Deoxy- or Oxy- forms released hemin during storage. Primary
structure strongly influenced Mb redox stability in the presence of
reactive secondary lipid oxidation products