• Food Science of Animal Resources
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• v.40 no.6
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• pp.969-979
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• 2020

Fresh grass carp was used to produce surimi and 50 g/kg, 100 g/kg, or 150 g/kg pork back fat was added. The water distribution, thiobarbituric acid reactive substances (TBARS), myoglobin oxidation, color parameter (L*, a*, and b*), heme and non-heme iron content of samples were determined to analyze the effects of different fat content on the oxidation of myoglobin and lipids during multiple freeze-thaw cycles of grass carp surimi. Both multiple freeze-thaw cycles and increased fat content lead to an increase in TBARS, a blue shift in the absorption peak of myoglobin porphyrin, a decrease in heme iron content, and an increase of non-heme iron content. Repeated freeze-thaw caused a decrease in immobilised water content and L*, and caused an increase in a* and b*. Increased fat content caused an increase in immobilised water content, L* and a*, and caused a decrease in b*.

• Animal Bioscience
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• v.34 no.8
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• pp.1382-1391
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• 2021

Objective: The objective was to evaluate the impact of different forms of iron including myoglobin, hemin, and ferric chloride on the quality of chicken breast meat. Methods: Chicken breast muscles were subjected to 1, 2, 3 mg/mL of FeCl₃, myoglobin and hemin treatment respectively, and the production of reactive oxygen species (ROS) and malondialdehyde, meat color, tenderness, water holding capacity and morphology of meat was evaluated. Results: Hemin was found to produce more ROS and induce greater extent of lipid oxidation than myoglobin and ferric chloride. However, it showed that hemin could significantly increase the redness and decrease the lightness of the muscle. Hemin was also shown to be prominent in improving water holding capacity of meat, maintaining a relatively higher level of the immobilized water from low-field nuclear magnetic resonance measurements. Morphology observation by hematoxylin-eosin staining further confirmed the results that hemin preserved the integrity of the muscle. Conclusion: The results indicated that hemin may have economic benefit for the industry based on its advantage in improving water holding capacity and quality of meat.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.2
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• pp.162-165
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• 2002

To determine changes of heme compounds on lipid oxidation during repeat heating in white muscled fish (yellowfin sole and yellow croaker), myoglobin, metmyoglobin, total iron, nonheme iron and heme iron contents were analysed. Myoglobin content was decreased in the step of repeat heating. Especially, it was decreased the most rapidly roasted at 180$^{\circ}C$ for 20 min in fillet samples. The skinless fillet roasted at the lower temperature resulted in the higher level of metmyoglobin associated with the reduced myoglobin. Regardless of roasted temperature and time, total iron content was not change in contrast of raw meat throughout processing. Nonheme iron content was increased, but heme iron content was decreased during roasted, heated and reheated.

• Food Science of Animal Resources
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• v.23 no.1
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• pp.86-95
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• 2003

Potential mechanisms by which vitamin E improves oxidative stability of myoglobin are documented. The basis by which this lipid-soluble antioxidant, ${\alpha}$-tocopherol, protects water-soluble oxymyoglobin is beginning to be understood. Recent evidence suggests that ${\alpha}$-tocopherol delays the release of prooxidative products of lipid oxidation from biomembranes, which in turn delays oxymyoglobin oxidation and the concomitant loss of desirable beef color. ${\alpha}$, ${\beta}$-Unsaturated aldehydes are one class of lipid oxidation products that enhance oxymyoglobin oxidation in vitro and appear to act by covalently binding to the protein. If ${\alpha}$-tocopherol delays the formation of these reactive aldehydes, then this could inhibit the prooxidative effect of these oxidation products toward oxymyoglobin. Additionally, ${\alpha}$-tocopherol may exert part of its color-stabilizing effect in beef by enhancing the metmyoglobin reduction.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.7
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• pp.1036-1043
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• 2019

Objective: To investigate the color and oxidative stabilities of longissimus lumborum (LL) and psoas major (PM) muscles from grain-finished Bos indicus cattle in Brazil. Methods: The LL and PM muscles were obtained 24 h post-mortem from eight (n = 8) Nellore bull carcasses, fabricated into 1.5-cm steaks, aerobically packaged, and stored at $4^{\circ}C$ for nine days. Steaks were analyzed for myoglobin concentration, pH, instrumental color, metmyoglobin reducing activity (MRA) and lipid oxidation. Results: The LL steaks exhibited greater (p<0.05) redness, color stability, and MRA than their PM counterparts on days 5 and 9. The LL and PM steaks demonstrated similar (p>0.05) lightness and yellowness on days 0, 5, and 9. On the other hand, PM steaks exhibited greater (p<0.05) myoglobin concentration, pH, and lipid oxidation than their LL counterparts. Conclusion: These results indicated that muscle source influenced the color and oxidative stabilities of beef from grain-finished Bos indicus animals. These results highlighted the necessity of muscle-specific strategies to improve the color stability of beef from grain-fed Bos indicus cattle.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2003.06a
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• pp.1-14
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• 2003

Lipid oxidation is one of the most important non-microbial causes of meat quality deterioration. However, there have been different/conflicting views concerning the primary catalysts of lipid oxidation in meat. This presentation provides brief overviews of lipid oxidation mechanism in general and catalysis of lipid oxidation in meat, and then focuses on inter-species differences in lipid oxidation potential, using results from our studies on meats (beef, pork and chicken) at retail and the respective meats of uniform postmortem history. The inter-species differences have highlighted the relative roles of meat pigment (myoglobin) content, catalase activity, and the concentration of oxidation substrates (particularly polyunsaturated fatty acids) in determining the lipid oxidation potential of raw meat versus cooked meat.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.4
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• pp.483-488
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• 1998

In order to elucidate the effect of heme compounds on lipid oxidation in roasted and/or reheated mackerel and pacific saury, changes in myoglobin, metmyoglobin, total iron, nonheme iron and heme iron content were measured. Throughout the steps of roasting, heating and reheating, myoglobin content was decteased more rapidly roasted at $180^{\circ}C$ for 20 min in fillet samples than those roasted at $200^{\circ}C$ for 15 min or $220^{\circ}C$ for 10 min. When the skinless samples were roasted at $180^{\circ}C$ for 20 min, about $38\%$ of myoglobin in raw meat were remained. The skinless fillet roasted at the lower temperature resulted the higher level of metmyoglobin due to the reduced myoglobin. Regardless of roasted temperature and time, total iron content was retained the level of raw meat throughout processing. 2 times of nonheme iron content was noted in the skinless fillet samples roasted at $180^{\circ}C$ for 20 min. All samples, heme iron content was decreased much lower by roasted temperature and in absence of skin on fillet. It was decreased about $33\%$ when roasted at $180^{\circ}C$ for 20 min in the skinless fillet in case of pacific saury.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 1999.10a
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• pp.100-100
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• 1999

• Animal Bioscience
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• v.36 no.5
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• pp.785-796
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• 2023

Objective: We aimed to evaluate the color and oxidative stability of beef gluteus medius (GM) from cattle raised in organic and non-organic production systems. Methods: The GM samples (n = 10) were obtained from organic (ORG; n = 5) or nonorganic (NORG; n = 5) beef samples, sliced into 2.54-cm steaks, packaged in aerobic conditions, and stored for nine days at 4℃. ORG and NORG steaks were compared regarding myoglobin concentration, pH, instrumental color, delta E (ΔE), metmyoglobin reducing activity (MRA), and lipid oxidation on days 0, 5, and 9. Results: Feeding system did not influence (p>0.05) the myoglobin concentration. ORG steaks exhibited greater (p<0.05) meat pH, yellowness, and MRA, whereas NORG steaks exhibited greater (p<0.05) redness, chroma, R630/580, delta E, and lipid oxidation. ORG and NORG steaks exhibited similar (p>0.05) lightness and hue angle. During storage, ORG and NORG exhibited an increase in muscle pH, hue angle, and lipid oxidation; and a decrease (p<0.05) in redness, yellowness, chroma, and color stability (R630/580). Both samples exhibited a stable (p>0.05) pattern for lightness and MRA. Conclusion: Therefore, the production system can affect beef color and lipid stability during storage.

• Food Science and Preservation
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• v.19 no.3
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• pp.420-427
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• 2012

The objective of this research was to investigate the effect of immersion in Rhus verniciflua Stokes extract (RVSE) on the total reducing ability (TRA), protein oxidation and myoglobin oxidation of beef steak (Hanwoo longissimus muscle) stored with high oxygen-modified-atmosphere packaging (MAP) (HOMAP, 75% $O_2$+20% $CO_2$+5% $N_2$) and low oxygen-MAP (LOMAP, 0% $O_2$+20% $CO_2$+80% $N_2$) at $4^{\circ}C$ for nine days. RVSE induced TRA (p<0.05), metmyoglobin (MetMb) formation, and the CIE $H^{\circ}$ value but reduced the carbonyl content and R630-R580, as an index of the intensity of redness by oxymyoglobin, and the CIE $L^*$,$a^*$, and $C^*$ values. HOMAP maintained a lower TRA, MetMb concentration, and CIE $H^{\circ}$ value but had higher R630-R580 and CIE $L^*$, $a^*$, and $C^*$ values compared to LOMAP. Therefore, RVSE induced TRA and protein oxidation stability but reduced myoglobin stability in Hanwoo beef steak. In addition, the effects of HOMAP were opposite those of RVSE.