Mass spectrometric characterization and thermostability of turkey myoglobin

LWT

Volumn 43, Issue 2, 2010, Pages 273-278

  Joseph, P ^a   Suman, S P ^a   Li, S ^a   Beach, C M ^b   Claus, J R ^c  

^a UNIVERSITY OF KENTUCKY   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

Mass spectrometry; Meleagris gallopavo; Myoglobin; Pink color defect; Thermostability; Turkey

Indexed keywords

BEEF; DEFECTS; MOLECULAR MASS; STABILITY;

CONDITION; MATRIX-ASSISTED LASER DESORPTION/IONIZATION-TIME-OF-FLIGHT MASS SPECTROMETRY; MELEAGRI GALLOPAVO; MOLECULAR BASIS; MYOGLOBIN; PINK COLOR; PINK COLOR DEFECT; PRIMARY STRUCTURES; QUALITY PROBLEMS; TURKEY;

MASS SPECTROMETRY;

MELEAGRIS GALLOPAVO;

EID: 70350571182     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2009.08.019     Document Type: Article

References (51)

1. Alderton A.L., Faustman C., Liebler D.C., and Hill D.W. Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal. Biochemistry 42 (2003) 4398-4405
2. Brown W.D., and Dolev A. Autoxidation of beef and tuna oxymyoglobins. Journal of Food Science 28 (1963) 207-210
3. Brown W.D., and Mebine L.B. Autoxidation of oxymyoglobin. Journal of Biological Chemistry 244 (1969) 6696-6701
4. Carbone D.L., Doorn J.A., Kiebler Z., and Petersen D.R. Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase. Chemical Research in Toxicology 18 (2005) 1324-1331
5. Chow C.J. Relationship between the stability and autoxidation of myoglobin. Journal of Agricultural and Food Chemistry 39 (1991) 22-26
6. Cornforth D.P., Rabovitser J.K., Ahuja S., Wagner J.C., Hanson R., Cummings B., et al. Carbon monoxide, nitric oxide, and nitrogen dioxide levels in gas ovens related to surface pinking of cooked beef and turkey. Journal of Agricultural and Food Chemistry 46 (1998) 255-261
7. Cornforth D.P., Vahabzadeh F., Carpenter C.E., and Bartholomew D.T. Role of reduced hemochromes in pink color defect of cooked turkey rolls. Journal of Food Science 51 (1986) 1132-1135
8. Cornish D.G., and Froning G.W. Isolation and purification of turkey heme proteins. Poultry Science 53 (1974) 365-377
9. Dautrevaux M., Boulanger Y., Han K., and Biserte G. Covalent structure of horse myoglobin. European Journal of Biochemistry 11 (1969) 267-277
10. Deconinck M., Peiffer S., Depreter J., Paul C., Schnek A.G., and Leonis J. The primary sequence of chicken myoglobin (Gallus gallus). Biochimica et Biophysica Acta 386 (1975) 567-575
11. Dosi R., Di Maro A., Chambery A., Colonna G., Costantini S., Geraci G., et al. Characterization and kinetics studies of water buffalo (Bubalus bubalis) myoglobin. Comparative Biochemistry and Physiology, Part B: Biochemistry and Molecular Biology 145 (2006) 230-238
12. Eich R.F., Li T., Lemon D.D., Doherty D.H., Curry S.R., Aitken J.F., et al. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 35 (1996) 6976-6983
13. Enoki Y., Ohga Y., Ishidate H., and Morimoto T. Primary structure of myoglobin from 31 species of birds. Comparative Biochemistry and Physiology, Part B 149 (2008) 11-21
14. Faustman C., and Phillips A.L. Measurement of discoloration in fresh meat. Current protocol in food analytical chemistry (2001), Wiley and Sons, New York
15. Gatellier P., Hamelin C., Durand Y., and Renerre M. Effect of a dietary vitamin E supplementation on color stability and lipid oxidation of air- and modified atmosphere-packaged beef. Meat Science 59 (2001) 133-140
16. Girard B., Vanderstoep J., and Richards J.F. Characterization of the residual pink color in cooked turkey breast and pork loin. Journal of Food Science 55 (1990) 1249-1254
17. Gu, S., Chen, D., Yin, S., Tang, K., & Sun, Q. (2007). Analysis of cDNA sequence of yak myoglobin and its oxidation in muscles. In Proceedings of 53rd international congress of meat science and technology (pp. 223-224), 5-10 August, 2007, Beijing, China.
18. Han K., Dautrevaux M., Chaila X., and Biserte G. The covalent structure of beef heart myoglobin. European Journal of Biochemistry 16 (1970) 465-471
19. Han K., Tetaert D., Moschetto Y., Dautrevaux M., and Kopeyan C. The covalent structure of sheep-heart myoglobin. European Journal of Biochemistry 27 (1972) 585-592
20. Holownia K., Chinnan M.S., and Reynolds A.E. Pink color defect in poultry white meat as affected by endogenous conditions. Journal of Food Science 68 (2003) 742-747
21. Janky D.M., and Froning G.W. The effect of pH and certain additives on heat denaturation of turkey meat myoglobin. Poultry Science 52 (1973) 152-159
22. Livingston D.J., and Brown W.D. The chemistry of myoglobin and its reaction. Food Technology 35 (1981) 244-252
23. Machlik, S. M. (1965). The effect of heat on bovine myoglobin derivatives in model systems and in beef semitendinosus muscle. Ph.D. Dissertation, Purdue University.
24. Manza L.L., Stamer S.L., Ham A.J., Codreanu S.G., and Liebler D.C. Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 5 (2005) 1742-1745
25. Miyazaki K., Uchida T., and Tsugita A. Molecular evolution of avian myoglobins from seven species in six different orders including three newly sequenced myoglobins from Japanese goshawk, spot-billed duck and thick-billed murre. Research Communications in Biochemistry and Cell and Molecular Biology 2 (1998) 91-103
26. Nalivka J. Meat and poultry facts (2003), American Meat Institute, Washington, DC
27. Nam K.C., and Ahn D.U. Carbon monoxide-heme pigment is responsible for the pink color in irradiated raw turkey breast meat. Meat Science 60 (2002) 25-33
28. National Turkey Federation (2008). http://www.eatturkey.com Accessed 11.10.08
29. Niewiarowicz A., Pikul J., and Czajka P. Gehalt an myoglobin und hemoglobin in fleisch verschiedener geflugelarten. Fleischwirtschaft 66 (1986) 1281-1282
30. Ponce-Alquicira E., and Taylor A.J. Extraction and ESI-CID-MS/MS analysis of myoglobins from different meat species. Food Chemistry 69 (2000) 81-86
31. Rousseaux J., Dautrevaux M., and Han K. Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobin. Biochimica et Biophysica Acta 439 (1976) 55-62
32. Sammel L.M., and Claus J.R. Citric acid and sodium citrate effects on reducing pink color defect of cooked intact turkey breasts and ground turkey rolls. Journal of Food Science 68 (2003) 874-878
33. Sammel L.M., and Claus J.R. Calcium chloride and tricalcium phosphate effects on the pink color defect in cooked ground and intact turkey breast. Meat Science 77 (2007) 492-498
34. SAS. SAS system for windows: Release 9.1 (2007), SAS Institute Inc., Cary, NC
35. Satterlee L.D., and Snyder H. Isoelectric fractionation of bovine metmyoglobin. Journal of Chromatography 41 (1969) 417-422
36. Sepe H.A., Faustman C., Lee S., Tang J., Suman S.P., and Venkitanarayanan K.S. Effects of reducing agents on premature browning in ground beef. Food Chemistry 93 (2005) 571-576
37. Suman S.P., Faustman C., Stamer S.L., and Liebler D.C. Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4 °C. Journal of Agricultural and Food Chemistry 54 (2006) 3402-3408
38. Suman S.P., Faustman C., Stamer S.L., and Liebler D.C. Proteomics of lipid oxidation-induced oxidation in porcine and bovine oxymyoglobins. Proteomics 7 (2007) 628-640
39. Suman S.P., Joseph P., Li S., Steinke L., and Fontaine M. Primary structure of goat myoglobin. Meat Science 82 (2009) 456-460
40. Swiss Institute of Bioinformatics, University of Geneva, Switzerland. http://www.expasy.org Accessed 11.10.08.
41. Tamburrini M., Romano M., Giardina B., and di Prisco G. The myoglobin of emperor penguin (Aptenodytes forsteri): amino acid sequence and functional adaptation to extreme conditions. Comparative Biochemistry and Physiology, Part B 122 (1999) 235-240
42. Tang J., Faustman C., and Hoagland T.A. Krzywicki revisited: equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science 69 (2004) C717-C720
43. Taylor A.J., Linforth R., Weir O., Hutton T., and Green B. Potential of electrospray mass spectrometry for meat pigment identification. Meat Science 33 (1993) 75-83
44. Trout G.R. Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate, and cooking temperature. Journal of Food Science 54 (1989) 536-544
45. Ueki N., Chow C.J., and Ochiai Y. Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship. Journal of Agricultural and Food Chemistry 53 (2005) 4968-4975
46. Ueki N., and Ochiai Y. Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish. Fisheries Science 70 (2004) 875-884
47. Ueki N., and Ochiai Y. Structural stabilities of recombinant scombridae fish myoglobins. Bioscience, Biotechnology, and Biochemistry 69 (2005) 1935-1943
48. Ueki N., and Ochiai Y. Effect of amino acid replacements on the structural stability of fish myoglobin. Journal of Biochemistry 140 (2006) 649-656
49. USDA. USDA advises consumers to use a meat thermometer when cooking hamburger. FSIS News and Information Bulletin (1997), FSIS, USDA, Washington DC
50. USDA-NASS. USDA-NASS agricultural statistics (2008). http://www.nass.usda.gov/index.asp Accessed 11.10.08
51. Votsch W., and Anderer F.A. The amino acid sequence of myoglobin from skeletal muscles of red deer (Cervus elaphus). Journal of Molecular Evolution 5 (1975) 315-326