Primary structure of turkey myoglobin

Joseph, P.; Suman, Surendranath P.; Li, Shuting; Claus, J.; Fontaine, Michele; Steinke, Laurey

doi:10.1016/j.foodchem.2011.04.024

Cited by 16 publications

(5 citation statements)

References 28 publications

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“…The results also showed a greater thermal stability inherent in turkey Mb, in contrast to beef Mb, and indicated that this is a major contributor to PCD (Joseph et al, 2010). Moreover, because turkey and chicken Mb share 100% similarity in their primary structure (Joseph et al, 2011), the aforementioned finding explains why PCD is observed primarily in these two poultry species (Holownia et al, 2003a).…”

Section: Cooked Color Phenomena In Poultrymentioning

confidence: 83%

“…Thus, Mb primary structure governs the resistance to heat-induced denaturation and influences the color of cooked meats. Comparative studies on thermal stabilities of turkey and beef Mb (Joseph, Suman, Li, Beach, & Claus, 2010;Joseph et al, 2011) demonstrated that replacement of smaller amino acids in the primary structure with larger ones in turkey Mb is partially responsible for its greater thermal stability than beef Mb.…”

Section: Primary Structure Of Mbmentioning

confidence: 99%

“…Comparative studies (Joseph et al, 2010; on the thermal stability and biochemistry of turkey and beef Mb have shown that the molecular mass of turkey Mb is 350 Da greater than beef Mb (Figure 3; Joseph et al, 2010). Joseph et al (2011) reported that several amino acids in turkey Mb are larger than those in beef Mb, which may contribute to the increased thermal stability of turkey Mb. The results also showed a greater thermal stability inherent in turkey Mb, in contrast to beef Mb, and indicated that this is a major contributor to PCD (Joseph et al, 2010).…”

Section: Cooked Color Phenomena In Poultrymentioning

confidence: 99%

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Factors influencing internal color of cooked meats

Suman

Nair

Joseph³

et al. 2016

Meat Science

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This manuscript overviews the pertinent research on internal color of uncured cooked meats, biochemical processes involved in meat cookery, and fundamental mechanisms governing myoglobin thermal stability. Heat-induced denaturation of myoglobin, responsible for the characteristic dull-brown color of cooked meats, is influenced by a multitude of endogenous (i.e., pH, muscle source, species, redox state) and exogenous (i.e., packaging, ingredients, storage) factors. The interactions between these factors critically influence the internal cooked color and can confuse the consumers, who often perceive cooked color to be a reliable indicator for doneness and safety. While certain phenomena in cooked meat color are cosmetic in nature, others can mislead consumers and result in foodborne illnesses. Research in meat color suggests that processing technologies and cooking practices in industry as well as households influence the internal cooked color. Additionally, the guidelines of many international public health and regulatory authorities recommend using meat thermometers to determine safe cooking endpoint temperature and to ensure product safety.

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Section: Cooked Color Phenomena In Poultrymentioning

confidence: 83%

Section: Primary Structure Of Mbmentioning

confidence: 99%

Section: Cooked Color Phenomena In Poultrymentioning

confidence: 99%

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Factors influencing internal color of cooked meats

Suman

Nair

Joseph³

et al. 2016

Meat Science

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“…Since the meat color, largely depending on Mb, is one of the properties that mostly influences the market value and consumer's purchase decision, many researches have been recently focused on the structural and functional characterization of Mb heme‐proteins from these birds. In particular, Japanese quail and northern bobwhite (Goodson, Beckstead, Payne, Singh, & Mohan, ), turkey (Joseph et al, ), ostrich (Dosi et al, ), and emu (Suman et al, ) Mbs have been characterized in the last years.…”

Section: Introductionmentioning

confidence: 99%

Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

et al. 2017

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Myoglobin (Mb) is a monomeric hemoprotein involved in dioxygen storage and transport in skeletal muscles and heart. Mb, containing the heme pigment, is present in large amount in meat, thus influencing meat color and consumer choice. Here, the primary structure of Mb isolated from muscle of Phasianus colchicus L. was determined by using a comparative peptide mapping approach based on MALDI-TOF mass spectrometry. This strategy allowed the determination of common pheasant Mb primary sequence, which resulted identical to the chicken Mb, as also confirmed by intact molecular mass determination by ESI/Q-TOF mass spectrometry. Indeed, the accurate molecular mass (17,290.50 Da) of common pheasant Mb was found to be in good agreement with that of chicken Mb (17,290.86 Da). Finally, the 3D model of common pheasant Mb was predicted by homology modeling. Overall, in this study we confirmed that chicken, turkey and common pheasant, belonging to the Galliformes order, share the same Mb sequence. Practical applicationsConsidering the economic importance of game meat consumption, our result may be interesting for meat industry, providing useful information for the determination of species-specific differences in color and color stability compared to other poultry species.

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“…Myoglobin (MG) can be considered to be a relevant marker for the immunodetection of pork. This cytoplasmic hemoprotein has been expressed in skeletal muscles and cardiac myocytes and has demonstrated significant variability of amino acid sequences for different species [19,20]. Kotoura et al used MG as a marker for the ELISA of beef content in meat products [21].…”

Section: Introductionmentioning

confidence: 99%

Immunochromatographic Detection of Myoglobin as a Specific Biomarker of Porcine Muscle Tissues in Meat Products

et al. 2020

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An immunochromatographic detection of myoglobin (MG) as a specific marker of porcine muscle tissue has been developed. The method is based on the sandwich lateral flow immunoassay (LFIA) with gold nanoparticles (AuNPs) as a label. The developed test system determines MG with a detection limit of 5 ng mL−1 within 15 min. A specific determination of porcine MG and no cross-reactivity with MG from other tested mammals and bird species was demonstrated. The test system is able to detect pork additives, as low as 0.01% (w/w), in minced beef. A technique of MG extraction from muscle tissue has been proposed which allows for rapid and efficient MG extraction from meat samples (within 20 min). The developed test system can serve as an effective means of controlling the authenticity and quality of meat products.

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Primary structure of turkey myoglobin

Cited by 16 publications

References 28 publications

Factors influencing internal color of cooked meats

Factors influencing internal color of cooked meats

Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

Immunochromatographic Detection of Myoglobin as a Specific Biomarker of Porcine Muscle Tissues in Meat Products

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