The Concentration of Myoglobin and Hemoglobin in Tuna Flesh

Brown, W. Duane

doi:10.1111/j.1365-2621.1962.tb00052.x

Cited by 45 publications

(20 citation statements)

References 8 publications

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“…Dark muscle, both superficial and deepseated, contained more hemoglobin, myoglobin and cytochrome c than the ordinary muscles (Sikorski et al, 1990). Muscle of yellowfin tuna contained myoglobin ranging from 37 to 128 mg% in light muscle and 530-2440 mg% in dark muscle (Brown, 1961). Sardine dark muscle comprised myoglobin 2.9 times greater than mackerel dark muscle.…”

Section: Chemical Compositions and Myoglobin In Sardine And Mackerel mentioning

confidence: 99%

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Chaijan

Benjakul

Visessanguan

et al. 2004

Food Research International

143

116

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Section: Chemical Compositions and Myoglobin In Sardine And Mackerel mentioning

confidence: 99%

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Chaijan

Benjakul

Visessanguan

et al. 2004

Food Research International

143

116

View full text Add to dashboard Cite

“…Previous studies reported that the structural stabilities of scombridae fish Mbs clearly differ among species, although the sequence identities of amino acids were in the range of 91 − 99% (Ueki et al, 2004;2005;2006). Among them, skipjack tuna Mb was the most thermostable, and bullet tuna (Auxis rochei) Mb showed the lowest stability.…”

Section: Resultsmentioning

confidence: 99%

“…Mb concentration is also an excellent parameter of meat quality grade. Mb concentration should be very similar in a given species (Brown, 2006); therefore, it is likely that Mb was partially denatured and insolubilized. The extractability of Mb was reduced in lower grades of meat.…”

Section: Resultsmentioning

confidence: 99%

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

Nurilmala

Ushio

Kaneko

et al. 2013

FSTR

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Four quality grades (excellent, good, acceptable, and "not acceptable") of yellowfin tuna meat (Thunnus albacares), as judged by a professional appraiser, were compared based on the red/ox state and extractability of myoglobin (Mb). As a result, the metMb ratio of the "not acceptable" grade of meat was significantly higher than that of the other higher-grade samples. In contrast, the highest ratio of oxyMb was found in the "excellent" meat, followed by good > acceptable > "not acceptable" meats. Color measurement revealed significant differences in a* value between the different grades of meat, but showed essentially no difference in L* and b* values. Both a* value and redness index (a*/b*) showed high correlation coefficients with metMb ratio. Mb extractability tended to be higher in the higher grade of meat. In conclusion, the commercial appraisal of tuna meat quality was demonstrated to be reliable. Keywords: tuna, meat, quality, color, myoglobin *To whom correspondence should be addressed. E-mail: aochiai@tokai-u.jp IntroductionSeven species of tunas are consumed around the world. Yellowfin tuna (Thunnus albacores), whose meat is characterized by a light red color and less fat, is one of the most commercially important and favored tuna species. This scombridae species inhabits tropical and subtropical waters around the world. Therefore, this species is generally exported to Japan from tropical countries, such as Indonesia, Taiwan, and so on (MMAF, 2012). A quality check is frequently performed before processing and transportation. Sensory analyses performed by experienced appraisers are generally carried out to determine freshness as a composite of qualitative traits. Color is one of the most important factors affecting consumer preferences. The meat color of tuna is closely related with myoglobin (Mb) content and the red/ox state of the heme iron.Mb is a small globular protein whose biological function is basically to temporarily store oxygen in skeletal and cardiac muscles for facilitation of respiration (Livingston et al., 1983), though new functions of Mb have been recently reported, such as nitrogen oxide scavenging activity (Cossins and Berenbrink, 2008;Flögel et al., 2010;Helbo et al., 2012). Generally, Mb content changes dependent on animal species, muscle part, age, and diet of the animal. Pale colored meat, such as chicken and pork, generally contain lower concentrations of Mb compared with red colored meat such as beef. Oxidative muscles, namely, slow skeletal muscle (including the dark muscle of fish) and heart muscle, contain abundant Mb. In scombridae fish such as tuna, abundant Mb is also found in fast skeletal muscle (also referred to as ordinary muscle, light muscle or white muscle).An iron atom of heme is placed in the hydrophobic region of Mb, binding the imidazole group of proximal histidine directly and distal histidine through a coordinate bond (Phillips and Schoenboen, 1981). The binding of oxygen, as well as the state of an iron atom in the heme pocket, contributes to the meat colo...

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“…Tilapias are partly distributed as skinned fillets packed in transparent plastic bags, and so the color of the dark muscle is crucial to the commercial value of the product. The redness of this muscle is mainly due to the presence of a pigment protein, myoglobin (Mb) [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Effects of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage

et al. 2009

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Discoloration profiles of dark muscle of skinned tilapia fillets were examined during iced storage after pretreatment with lactic acid (LA) or sodium carbonate (SC). During the subsequent storage, the a* values decreased gradually, and changed more rapidly when the pH was lower than 6.3. The fillet pretreated with 10% (v/v) LA exhibited the highest metmyoglobin formation ratio (MetMb%), followed by the fillet pretreated with 5% (v/v) LA, the control fillet, and the fillet pretreated with 10% (w/ v) SC. The sample pretreated with 10% LA showed a marked decrease in the a* value. Discoloration of the control was not observed until the ninth day of iced storage, and no discoloration was observed up to the 11th day for the fillet pretreated with 10% SC. These fillet discoloration profiles were subsequently verified using the myoglobin (Mb) fraction prepared from the dark muscle. MetMb% of the Mb fraction gradually increased during storage, and this increase accelerated at pH values of \6.3. Discoloration of the Mb fraction also showed a similar tendency, and no significant discoloration was observed at pH values of [6.5. These results suggest that pH greatly affects the discoloration rate of the dark muscle of skinned fillet, and the critical pH for the accelerated autooxidation of tilapia Mb is in the range 6.3-6.5.

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The Concentration of Myoglobin and Hemoglobin in Tuna Flesh

Cited by 45 publications

References 8 publications

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

Effects of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage

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