Lipid oxidation-induced oxidation in emu and ostrich myoglobins

M. N. Nair; S. P. Suman; S. Li; P. Joseph; C. M. Beach

doi:10.1016/j.meatsci.2013.08.029

Lipid oxidation-induced oxidation in emu and ostrich myoglobins

M. N. Nair, S. P. Suman, S. Li, P. Joseph, C. M. Beach

Producción científica: Article › revisión exhaustiva

37 Citas (Scopus)

Resumen

Emu and ostrich are ratites gaining increasing popularity as sources of low-fat meats. Secondary products of lipid oxidation, such as 4-hydroxy-2-nonenal (HNE), compromise myoglobin redox stability in a species-specific manner. However, the molecular basis of lipid oxidation-induced oxidation in ratite myoglobins has not been investigated. Therefore, our objective was to characterize lipid oxidation-induced oxidation in ratite myoglobins, in comparison with beef myoglobin. At physiological condition (pH. 7.4, 37. °C) HNE accelerated (P<. 0.05) oxidation of emu, ostrich, and beef oxymyoglobins. Autoxidation and HNE-induced oxidation were greater (P<. 0.05) in ostrich oxymyoglobin than in emu and beef oxymyoglobins. Mass spectrometric analyses revealed that HNE formed mono-adduct with both emu and ostrich myoglobins after 6. h of incubation. Tandem mass spectrometry demonstrated that HNE adducted histidine 36 in ostrich myoglobin, whereas histidines 34 and 36 were adducted in emu myoglobin. The results indicate that primary structure of ratite myoglobins influences their redox stability in the presence of prooxidants.

Idioma original	English
Páginas (desde-hasta)	984-993
Número de páginas	10
Publicación	Meat Science
Volumen	96
N.º	2
DOI	https://doi.org/10.1016/j.meatsci.2013.08.029
Estado	Published - feb 2014

Nota bibliográfica

Funding Information:
This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research .

Financiación

This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research .

Financiadores	Número del financiador
Office of the Vice President for Research
University of Kentucky
Kentucky Agricultural Experiment Station

ASJC Scopus subject areas

Food Science

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10.1016/j.meatsci.2013.08.029

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title = "Lipid oxidation-induced oxidation in emu and ostrich myoglobins",

abstract = "Emu and ostrich are ratites gaining increasing popularity as sources of low-fat meats. Secondary products of lipid oxidation, such as 4-hydroxy-2-nonenal (HNE), compromise myoglobin redox stability in a species-specific manner. However, the molecular basis of lipid oxidation-induced oxidation in ratite myoglobins has not been investigated. Therefore, our objective was to characterize lipid oxidation-induced oxidation in ratite myoglobins, in comparison with beef myoglobin. At physiological condition (pH. 7.4, 37. °C) HNE accelerated (P<. 0.05) oxidation of emu, ostrich, and beef oxymyoglobins. Autoxidation and HNE-induced oxidation were greater (P<. 0.05) in ostrich oxymyoglobin than in emu and beef oxymyoglobins. Mass spectrometric analyses revealed that HNE formed mono-adduct with both emu and ostrich myoglobins after 6. h of incubation. Tandem mass spectrometry demonstrated that HNE adducted histidine 36 in ostrich myoglobin, whereas histidines 34 and 36 were adducted in emu myoglobin. The results indicate that primary structure of ratite myoglobins influences their redox stability in the presence of prooxidants.",

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author = "Nair, \{M. N.\} and Suman, \{S. P.\} and S. Li and P. Joseph and Beach, \{C. M.\}",

note = "Funding Information: This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research .",

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language = "English",

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AU - Nair, M. N.

AU - Suman, S. P.

AU - Li, S.

AU - Joseph, P.

AU - Beach, C. M.

N1 - Funding Information: This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research .

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N2 - Emu and ostrich are ratites gaining increasing popularity as sources of low-fat meats. Secondary products of lipid oxidation, such as 4-hydroxy-2-nonenal (HNE), compromise myoglobin redox stability in a species-specific manner. However, the molecular basis of lipid oxidation-induced oxidation in ratite myoglobins has not been investigated. Therefore, our objective was to characterize lipid oxidation-induced oxidation in ratite myoglobins, in comparison with beef myoglobin. At physiological condition (pH. 7.4, 37. °C) HNE accelerated (P<. 0.05) oxidation of emu, ostrich, and beef oxymyoglobins. Autoxidation and HNE-induced oxidation were greater (P<. 0.05) in ostrich oxymyoglobin than in emu and beef oxymyoglobins. Mass spectrometric analyses revealed that HNE formed mono-adduct with both emu and ostrich myoglobins after 6. h of incubation. Tandem mass spectrometry demonstrated that HNE adducted histidine 36 in ostrich myoglobin, whereas histidines 34 and 36 were adducted in emu myoglobin. The results indicate that primary structure of ratite myoglobins influences their redox stability in the presence of prooxidants.

AB - Emu and ostrich are ratites gaining increasing popularity as sources of low-fat meats. Secondary products of lipid oxidation, such as 4-hydroxy-2-nonenal (HNE), compromise myoglobin redox stability in a species-specific manner. However, the molecular basis of lipid oxidation-induced oxidation in ratite myoglobins has not been investigated. Therefore, our objective was to characterize lipid oxidation-induced oxidation in ratite myoglobins, in comparison with beef myoglobin. At physiological condition (pH. 7.4, 37. °C) HNE accelerated (P<. 0.05) oxidation of emu, ostrich, and beef oxymyoglobins. Autoxidation and HNE-induced oxidation were greater (P<. 0.05) in ostrich oxymyoglobin than in emu and beef oxymyoglobins. Mass spectrometric analyses revealed that HNE formed mono-adduct with both emu and ostrich myoglobins after 6. h of incubation. Tandem mass spectrometry demonstrated that HNE adducted histidine 36 in ostrich myoglobin, whereas histidines 34 and 36 were adducted in emu myoglobin. The results indicate that primary structure of ratite myoglobins influences their redox stability in the presence of prooxidants.

KW - Lipid oxidation

KW - Mass spectrometry

KW - Myoglobin

KW - Ratite

KW - Redox stability

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Lipid oxidation-induced oxidation in emu and ostrich myoglobins

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