Interaction of Fish Myoglobin and Myofibrillar Proteins

Chaijan, Manat; Benjakul, S.; Visessanguan, Wonnop; Lee, S.; Faustman, C.

doi:10.1111/j.1750-3841.2008.00749.x

Cited by 17 publications

(17 citation statements)

References 24 publications

(27 reference statements)

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“…This suggested that interactions between MP and SP resulted in increased thermal stability of protein in the system. One of the sarcoplasmic protein, myoglobin, was reported to interact with the tail portion of MHC during incubation at 4 °C for 6 h (Chaijan et al ., ). The interactions were dependent on NaCl concentration and could be occurred at the NaCl concentration used in this study (0.3 m NaCl; Hemung & Chin, ).…”

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 97%

“…The discrepancy of the two studies might be partially due to the different protein and moisture contents. In previous study, the oxidation of myogen also resulted in a dark colour (Chaijan et al, 2008). Ramirez et al (2007) found that addition of 5% recovered solid from the washed water, generated by a surimi plant, into surimi, decreased the redness.…”

Section: Colour Values Of Myofibrillar Proteins Gelmentioning

confidence: 90%

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Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Hemung

Chin

2014

Int J of Food Sci Tech

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Summary Fish sarcoplasmic protein (SP) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein (MP) with microbial transglutaminase (MTG). The denaturation temperature (Td) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH‐treated SPs, while the breaking forces were similar to control. The result indicated that pH‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties.

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 97%

Section: Colour Values Of Myofibrillar Proteins Gelmentioning

confidence: 90%

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Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Hemung

Chin

2014

Int J of Food Sci Tech

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“…It is likely that structural changes in the Mb in the dark muscle were largely responsible for the discoloration of tilapia fillet during iced storage. Under denaturing conditions, hydrophobic residues buried inside the Mb molecule could have been exposed at the surface, causing the aggregation of Mb itself or its adhesion to myofibrillar proteins [47].…”

Section: Discussionmentioning

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 mechanism responsible for Mb aggregation has been partly characterized; Mb itself tends to self-aggregate (Chow et al, 1989), whereas it has been reported that, in postmortem meat, Mb binds to myofibrillar proteins (Chajian et al, 2008) or reacts with fatty acids (Suman et al, 2007).…”

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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Interaction of Fish Myoglobin and Myofibrillar Proteins

Cited by 17 publications

References 24 publications

Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

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

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

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