Quantitative Estimations of Myoglobin and Hemoglobin in Beef Muscle Extracts

Fleming, H. P.; Blumer, T. N.; Craig, H. B.

doi:10.2527/jas1960.1941164x

Cited by 52 publications

(26 citation statements)

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“…The main iron-containing proteins in the water extracts from meat are the hemoproteins, Mb and Hb (Hunt and Hedrick, 1977;Hazell, 1982;Love, 1988). Beef has a higher pigment content than chicken (Fleming et al, 1960;Saffle, 1973) resulting in the higher watersoluble iron in raw beef longissimus muscle we found. The contents of water-soluble iron and insoluble iron of beef and chicken muscle followed similar patterns of change with temperature (Fig.…”

Section: Resultsmentioning

confidence: 73%

Iron Distribution in Heated Beef and Chicken Muscles

Han

McMillin

Godber

et al. 1993

Journal of Food Science

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Distribution of iron in six fractions (water-soluble, water-insoluble, diffusate, hematin, total heme, and ferritin) of beef and chicken muscles hcatcd to 55, 70, 85, and 100°C was determined. Iron content decreased in water-soluble fractions and increased in water-insoluble fractions as temperature increased from 27°C to 100°C. Heme iron decreased more from 55°C to 85°C than from 27°C to 55°C or 85°C to 100°C. The increase in diffusate iron appeared to be less than the decrease in heme iron at each heating temperature. As temperature increased from 27°C to IOtYC, hematin iron content increased and extractable ferritin iron content decreased. These findings may help explain rapid development of oxidative rancidity in cooked meat.

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Section: Resultsmentioning

confidence: 73%

Iron Distribution in Heated Beef and Chicken Muscles

Han

McMillin

Godber

et al. 1993

Journal of Food Science

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“…Hemoglobin (Hb) constitutes 5 to 30% of the total muscle pigments (Fleming et al, 1960;Rickansrud and Henrickson, 1967;Huffman, 1980;Niewiarowicz et al, 1986) depending on holding time and bleeding condition or methods, but in most cases Mb alone is used as an index of fresh meat color. The color of fresh meat varies not only with the number and amount of pigments present but also the state of the heme group of the pigments.…”

Section: Introductionmentioning

confidence: 99%

Effects of Added Pigments, Salt, and Phosphate on Color, Extractable Pigment, Total Pigment, and Oxidation-Reduction Potential in Turkey Breast Meat

Ahn

Maurer

1989

Poultry Science

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Ground turkey breast meat treatments were prepared with 16 combinations of myoglobin (0, .4 mg/g meat), cytochrome c (0, .1 mg/g meat), salt (NaCl; 1, 2.5%), and sodium tripolyphosphate (0, .5%) before cooking to determine their effect on meat color, water extractable pigments, total pigment, and oxidation-reduction potential in cooked turkey breast meat Addition of myoglobin did not increase extractable pigment but significantly (P<01) increased the redness (a-value) and total pigment of cooked meat Cytochrome c greatly increased both extractable pigment and a-values (P<.01). Most of the added myoglobin was denatured or became unextractable, but almost all of the added cytochrome c was extractable after cooking. A large portion of extractable pigment and drip was due to cytochrome c; added cytochrome c had a much stronger effect than myoglobin on pinkness of cooked turkey breast meat. Addition of pigments always decreased L-values (lightness) of breast meat. Salt significantly (P<.01) increased a-values and decreased L-and b-values (yellowness). Extractable pigment was increased by salt in all pigment treatments except myoglobin-added meat; total pigment was hardly affected by salt. Phosphate significantly (P<.01) increased a-values in no pigment and myoglobin-added meat, but was less effective than salt. Oxidationreduction potentials were decreased by adding salt and phosphate. Those potential changes could have a strong effect on pinkness of cooked turkey breast meat if the oxidation-reduction potentials of the meat are around +90 mV or -50 mV. (

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“…The wide range of Hb:Mb ratios previously reported for beef muscle (5)(6)(7)(8) warrants a reexamination into the relative amounts of these heme proteins that are present in the postmortem tissue, keeping in mind that Hb subunit formation occurs under conditions of extraction (e.g., dilution), which can cause Mb determinations to be errantly high. These subunits are also extremely prone to heme release, which will result in decreased recovery of the Hb present in the tissue.…”

mentioning

confidence: 96%

Pro-oxidative Characteristics of Trout Hemoglobin and Myoglobin: A Role for Released Heme in Oxidation of Lipids

Richards

Dettmann

Grunwald

2005

J. Agric. Food Chem.

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The molecular mass of trout myoglobin was 16017 Da based on electrospray ionization mass spectrometry. A Root effect (low oxygen affinity at pH 6.3) was determined in trout hemoglobin but not myoglobin. At pH 6.3, myoglobin autoxidized more rapidly (3.5-fold) as compared to anodic hemoglobin. Anodic hemoglobin was a better catalyst of lipid oxidation in washed cod muscle as compared to myoglobin at pH 6.3. This suggested that some process other than met heme protein formation was the rate-limiting step in lipid oxidation processes. Heme loss rates were determined using the apomyoglobin mutant H64Y prepared from sperm whale. Anodic hemoglobin released its heme group much more rapidly than myoglobin. In comparisons of anodic and cathodic hemoglobins, heme loss rate better predicted the onset of lipid oxidation than autoxidation rate. These studies collectively suggest that heme dissociation has a primary role in the ability of different heme proteins to promote lipid oxidation processes.

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Quantitative Estimations of Myoglobin and Hemoglobin in Beef Muscle Extracts

Cited by 52 publications

References 0 publications

Iron Distribution in Heated Beef and Chicken Muscles

Iron Distribution in Heated Beef and Chicken Muscles

Effects of Added Pigments, Salt, and Phosphate on Color, Extractable Pigment, Total Pigment, and Oxidation-Reduction Potential in Turkey Breast Meat

Pro-oxidative Characteristics of Trout Hemoglobin and Myoglobin: A Role for Released Heme in Oxidation of Lipids

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