Mass spectrometric characterization and thermostability of turkey myoglobin

Joseph, P.; Suman, Surendranath P.; Li, S.; Beach, Carol M.; Claus, J.

doi:10.1016/j.lwt.2009.08.019

Cited by 21 publications

(7 citation statements)

References 41 publications

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“…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.…”

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: Primary Structure Of Mbmentioning

confidence: 99%

Section: Cooked Color Phenomena In Poultrymentioning

confidence: 99%

Factors influencing internal color of cooked meats

Suman

Nair

Joseph³

et al. 2016

Meat Science

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“…Oxygenation of deoxyMb results in bright‐red meat due to the formation of MbO 2 , while oxidation of deoxyMb to MetMb causes brown discoloration . The reduction of MetMb influences meat color stability and increases the shelf life of fresh meat color . In this study, dietary CC increased the content of deoxyMb and decreased the content of MetMb, suggesting that the inhibition on MetMb generation by appropriate CC supplement could delay meat discoloration, although excess of CC may accelerate oxidation.…”

Section: Discussionmentioning

confidence: 58%

Effects of dietary coated cysteamine hydrochloride on pork color in finishing pigs

Bai

Liu²,

et al. 2017

J Sci Food Agric

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“…Turkey myoglobin was isolated from cardiac muscles according to Joseph et al (2010a) via ammonium sulphate precipitation and gel-filtration chromatography. The isolated myoglobin was further refined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) as described by Laemmli (1970) to ensure the purity.…”

Section: Isolation Of Turkey Myoglobinmentioning

confidence: 99%

“…Thermostability of big eye tuna myoglobin was lower than those of yellow fin and blue fin tuna myoglobins, albeit these molecules exhibit more than 95% similarity in amino acid sequence (Ueki & Ochiai, 2004). Joseph et al (2010a) determined that turkey myoglobin had a greater resistance to heat-induced denaturation than did beef myoglobin and, based on mass spectrometric data, these authors suggested that the primary structures of beef and turkey myoglobins could be different. In addition, the greater thermostability of turkey myoglobin, together with the inherently greater pH of turkey meat, compared to beef, was offered as a partial explanation for pink colour defect.…”

Section: Nomentioning

confidence: 99%