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Volumn 60, Issue 12, 2012, Pages 3196-3203

Proteomics of muscle-specific beef color stability

Author keywords

beef color; color stability; Longissimus lumborum; Psoas major; sarcoplasmic proteome

Indexed keywords

ALDOSE REDUCTASE; COLOR STABILITY; CREATINE KINASE; ENOLASE; HEAT-SHOCK; LIPID OXIDATION; LONGISSIMUS; METHIONINE SULFOXIDE REDUCTASE; MITOCHONDRIAL ACONITASE; NEGATIVE CORRELATION; POSITIVE CORRELATIONS; PROTEOME ANALYSIS; PROTEOMICS; PSOAS MAJOR; SARCOPLASMIC;

EID: 84859127509     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf204188v     Document Type: Article
Times cited : (217)

References (40)
  • 1
    • 22144493345 scopus 로고    scopus 로고
    • Current research in meat color
    • Mancini, R. A.; Hunt, M. C. Current research in meat color Meat Sci. 2005, 71, 100-121
    • (2005) Meat Sci. , vol.71 , pp. 100-121
    • Mancini, R.A.1    Hunt, M.C.2
  • 3
    • 84930481689 scopus 로고
    • The biochemical basis for discoloration in fresh meat: A review
    • Faustman, C.; Cassens, R. G. The biochemical basis for discoloration in fresh meat: a review J. Muscle Foods 1990, 1, 217-243
    • (1990) J. Muscle Foods , vol.1 , pp. 217-243
    • Faustman, C.1    Cassens, R.G.2
  • 4
    • 18844374883 scopus 로고    scopus 로고
    • Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles
    • McKenna, D. R.; Mies, P. D.; Baird, B. E.; Pfeiffer, K. D.; Ellebracht, J. W.; Savell, J. W. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles Meat Sci. 2005, 70, 665-682
    • (2005) Meat Sci. , vol.70 , pp. 665-682
    • McKenna, D.R.1    Mies, P.D.2    Baird, B.E.3    Pfeiffer, K.D.4    Ellebracht, J.W.5    Savell, J.W.6
  • 5
    • 33751305684 scopus 로고    scopus 로고
    • Color stability, reducing activity, and cytochrome c oxidase activity of five bovine muscles
    • Seyfert, M.; Mancini, R. A.; Hunt, M. C.; Tang, J.; Faustman, C.; Garcia, M. Color stability, reducing activity, and cytochrome c oxidase activity of five bovine muscles J. Agric. Food Chem. 2006, 54, 8919-8925
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 8919-8925
    • Seyfert, M.1    Mancini, R.A.2    Hunt, M.C.3    Tang, J.4    Faustman, C.5    Garcia, M.6
  • 6
    • 33845703550 scopus 로고    scopus 로고
    • Influence of carbon monoxide in package atmospheres containing oxygen on color, reducing activity, and oxygen consumption of five bovine muscles
    • Seyfert, M.; Mancini, R. A.; Hunt, M. C.; Tang, J.; Faustman, C. Influence of carbon monoxide in package atmospheres containing oxygen on color, reducing activity, and oxygen consumption of five bovine muscles Meat Sci. 2007, 75, 432-442
    • (2007) Meat Sci. , vol.75 , pp. 432-442
    • Seyfert, M.1    Mancini, R.A.2    Hunt, M.C.3    Tang, J.4    Faustman, C.5
  • 7
    • 0000670411 scopus 로고
    • Biochemical factors influencing metmyoglobin formation on beef from muscles of differing color stability
    • O'Keeffe, M.; Hood, D. E. Biochemical factors influencing metmyoglobin formation on beef from muscles of differing color stability Meat Sci. 1982, 7, 209-228
    • (1982) Meat Sci. , vol.7 , pp. 209-228
    • O'Keeffe, M.1    Hood, D.E.2
  • 8
    • 53349167520 scopus 로고    scopus 로고
    • Effect of carbon monoxide packaging and lactate-enhancement on the color stability of beef steaks stored at 1°C for 9 days
    • Mancini, R. A.; Suman, S. P.; Ramanathan, R.; Konda, M. R. Effect of carbon monoxide packaging and lactate-enhancement on the color stability of beef steaks stored at 1°C for 9 days Meat Sci. 2009, 81, 71-76
    • (2009) Meat Sci. , vol.81 , pp. 71-76
    • Mancini, R.A.1    Suman, S.P.2    Ramanathan, R.3    Konda, M.R.4
  • 9
    • 58149483487 scopus 로고    scopus 로고
    • Effect of lactate-enhancement, modified atmosphere packaging, and muscle source on the internal cooked color of beef steaks
    • Suman, S. P.; Mancini, R. A.; Ramanathan, R.; Konda, M. R. Effect of lactate-enhancement, modified atmosphere packaging, and muscle source on the internal cooked color of beef steaks Meat Sci. 2009, 81, 664-670
    • (2009) Meat Sci. , vol.81 , pp. 664-670
    • Suman, S.P.1    Mancini, R.A.2    Ramanathan, R.3    Konda, M.R.4
  • 11
    • 34547142184 scopus 로고    scopus 로고
    • Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period
    • Jia, X.; Ekman, M.; Grove, H.; Faergestad, E. M.; Aass, L.; Hildrum, K. I.; Hollung, K. Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period J. Proteome Res. 2007, 6, 2720-2731
    • (2007) J. Proteome Res. , vol.6 , pp. 2720-2731
    • Jia, X.1    Ekman, M.2    Grove, H.3    Faergestad, E.M.4    Aass, L.5    Hildrum, K.I.6    Hollung, K.7
  • 12
    • 67650541787 scopus 로고    scopus 로고
    • Peroxiredoxin-6: A potential protein marker for meat tenderness in bovine longissimus thoracis muscle
    • Jia, X.; Veiseth-Kent, E.; Grove, H.; Kuziora, P.; Aass, L.; Hildrum, K. I.; Hollung, K. Peroxiredoxin-6: A potential protein marker for meat tenderness in bovine longissimus thoracis muscle J. Anim. Sci. 2009, 87, 2391-2399
    • (2009) J. Anim. Sci. , vol.87 , pp. 2391-2399
    • Jia, X.1    Veiseth-Kent, E.2    Grove, H.3    Kuziora, P.4    Aass, L.5    Hildrum, K.I.6    Hollung, K.7
  • 13
    • 36749014526 scopus 로고    scopus 로고
    • Muscle proteome and meat eating qualities of Longissimus thoracis of "blonde d'Aquitaine" young bulls: A central role of HSP27 isoforms
    • Morzel, M.; Terlouw, C.; Chambon, C.; Micol, D.; Picard, B. Muscle proteome and meat eating qualities of Longissimus thoracis of "Blonde d'Aquitaine" young bulls: a central role of HSP27 isoforms Meat Sci. 2008, 78, 297-304
    • (2008) Meat Sci. , vol.78 , pp. 297-304
    • Morzel, M.1    Terlouw, C.2    Chambon, C.3    Micol, D.4    Picard, B.5
  • 14
    • 72449156073 scopus 로고    scopus 로고
    • Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization
    • Laville, E.; Sayd, T.; Morzel, M.; Blinet, S.; Chambon, C.; Lepetit, J.; Renand, G.; Hocquette, J. F. Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization J. Agric. Food Chem. 2009, 57, 10755-10764
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 10755-10764
    • Laville, E.1    Sayd, T.2    Morzel, M.3    Blinet, S.4    Chambon, C.5    Lepetit, J.6    Renand, G.7    Hocquette, J.F.8
  • 15
    • 5744228466 scopus 로고    scopus 로고
    • Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus
    • Hwang, I. H.; Park, B. I.; Kim, J. H.; Cho, S. H.; Lee, J. M. Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus Meat Sci. 2005, 69, 79-91
    • (2005) Meat Sci. , vol.69 , pp. 79-91
    • Hwang, I.H.1    Park, B.I.2    Kim, J.H.3    Cho, S.H.4    Lee, J.M.5
  • 16
    • 0030305937 scopus 로고    scopus 로고
    • Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin
    • Renerre, M.; Dumont, F.; Gatellier, P. Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin Meat Sci. 1996, 43, 111-121
    • (1996) Meat Sci. , vol.43 , pp. 111-121
    • Renerre, M.1    Dumont, F.2    Gatellier, P.3
  • 18
    • 0004210728 scopus 로고
    • AMSA. American Meat Science Association: Chicago, IL, USA.
    • AMSA. Guidelines for Meat Color Evaluation; American Meat Science Association: Chicago, IL, USA, 1991.
    • (1991) Guidelines for Meat Color Evaluation
  • 19
    • 0036265726 scopus 로고    scopus 로고
    • Comparison of assays for metmyoglobin reducing ability in beef inside and outside semimembranosus muscle
    • Sammel, L. M.; Hunt, M. C.; Kropf, D. H.; Hachmeister, K. A.; Johnson, D. E. Comparison of assays for metmyoglobin reducing ability in beef inside and outside semimembranosus muscle J. Food Sci. 2002, 67, 978-984
    • (2002) J. Food Sci. , vol.67 , pp. 978-984
    • Sammel, L.M.1    Hunt, M.C.2    Kropf, D.H.3    Hachmeister, K.A.4    Johnson, D.E.5
  • 21
    • 0001249258 scopus 로고
    • Evaluation of rapid tests for monitoring alterations in meat quality during storage. 1. Intact meat
    • Strange, E. D.; Benedict, R. C.; Smith, J. L.; Swift, L. E. Evaluation of rapid tests for monitoring alterations in meat quality during storage. 1. Intact meat J. Food Prot. 1977, 40, 843-847
    • (1977) J. Food Prot. , vol.40 , pp. 843-847
    • Strange, E.D.1    Benedict, R.C.2    Smith, J.L.3    Swift, L.E.4
  • 22
    • 35648952065 scopus 로고
    • The effects of α-tocopherol and ascorbate upon oxymyoglobin phospholipid oxidation
    • Yin, M. C.; Faustman, C.; Riesen, J. W.; Williams, S. N. The effects of α-tocopherol and ascorbate upon oxymyoglobin phospholipid oxidation J. Food Sci. 1993, 58, 1273-1276
    • (1993) J. Food Sci. , vol.58 , pp. 1273-1276
    • Yin, M.C.1    Faustman, C.2    Riesen, J.W.3    Williams, S.N.4
  • 23
    • 77956892162 scopus 로고    scopus 로고
    • release 9.2; SAS Institute Inc. Cary, NC.
    • SAS System for Windows, release 9.2; SAS Institute Inc.: Cary, NC, 2009.
    • (2009) SAS System for Windows
  • 24
    • 0037461349 scopus 로고    scopus 로고
    • Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal
    • Alderton, A. L.; Faustman, C.; Liebler, D. C.; Hill, D. W. Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal Biochemistry 2003, 42, 4398-4405
    • (2003) Biochemistry , vol.42 , pp. 4398-4405
    • Alderton, A.L.1    Faustman, C.2    Liebler, D.C.3    Hill, D.W.4
  • 25
    • 77954387450 scopus 로고    scopus 로고
    • Myoglobin and lipid oxidation interactions: Mechanistic bases and control
    • Faustman, C.; Sun, Q.; Mancini, R. A.; Suman, S. P. Myoglobin and lipid oxidation interactions: Mechanistic bases and control Meat Sci. 2010, 86, 86-94
    • (2010) Meat Sci. , vol.86 , pp. 86-94
    • Faustman, C.1    Sun, Q.2    Mancini, R.A.3    Suman, S.P.4
  • 29
    • 0141510042 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins during recovery after oxidative stress: Only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress
    • Chevallet, M.; Wagner, E.; Luche, S.; Van Dorsselaer, A.; Leize-Wagner, E.; Rabilloud, T. Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress J. Biol. Chem. 2003, 278, 37146-37153
    • (2003) J. Biol. Chem. , vol.278 , pp. 37146-37153
    • Chevallet, M.1    Wagner, E.2    Luche, S.3    Van Dorsselaer, A.4    Leize-Wagner, E.5    Rabilloud, T.6
  • 30
    • 0034467710 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: Biochemistry and physiological role
    • Brot, N.; Weissbach, H. Peptide methionine sulfoxide reductase: biochemistry and physiological role Biopolymers 2000, 55, 288-296
    • (2000) Biopolymers , vol.55 , pp. 288-296
    • Brot, N.1    Weissbach, H.2
  • 31
    • 77954385948 scopus 로고    scopus 로고
    • High-oxygen modified atmosphere packaging system induces lipid and myoglobin oxidation and protein polymerization
    • Kim, Y. H.; Huff-Lonergan, E.; Sebranek, J. G.; Lonergan, S. M. High-oxygen modified atmosphere packaging system induces lipid and myoglobin oxidation and protein polymerization Meat Sci. 2010, 85, 759-767
    • (2010) Meat Sci. , vol.85 , pp. 759-767
    • Kim, Y.H.1    Huff-Lonergan, E.2    Sebranek, J.G.3    Lonergan, S.M.4
  • 32
    • 77954383543 scopus 로고    scopus 로고
    • Review: Theoretical aspects of water-holding in meat
    • Puolanne, E.; Halonen, M. Review: Theoretical aspects of water-holding in meat Meat Sci. 2010, 86, 151-165
    • (2010) Meat Sci. , vol.86 , pp. 151-165
    • Puolanne, E.1    Halonen, M.2
  • 33
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: Biological consequences
    • Stadtman, E. R.; Moskovitz, J.; Levine, R. L. Oxidation of methionine residues of proteins: biological consequences Antioxid. Redox Signal. 2003, 5, 577-582
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 34
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman, E. R. Protein oxidation and aging Free Radical Res. 2006, 40, 1250-1258
    • (2006) Free Radical Res. , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 36
    • 73049121498 scopus 로고
    • Systematic analytical differences between Psoas major and Longissimus dorsi muscle of cattle
    • Lawrie, R. A. Systematic analytical differences between Psoas major and Longissimus dorsi muscle of cattle Br. J. Nutr. 1961, 15, 453
    • (1961) Br. J. Nutr. , vol.15 , pp. 453
    • Lawrie, R.A.1
  • 37
    • 77953144809 scopus 로고    scopus 로고
    • Potential roles of lactate, pyruvate, succinate, and citrate in beef color
    • In, June 2009, Rogers, AR; American Meat Science Association: Champaign, IL
    • Mancini, R. A.; Ramanathan, R. Potential roles of lactate, pyruvate, succinate, and citrate in beef color. In Proceedings of the 62nd Reciprocal Meat Conference, June 2009, Rogers, AR; American Meat Science Association: Champaign, IL, 2009; pp 71-75.
    • (2009) Proceedings of the 62nd Reciprocal Meat Conference , pp. 71-75
    • Mancini, R.A.1    Ramanathan, R.2
  • 39
    • 5444224007 scopus 로고    scopus 로고
    • Proteomics approach in meat science: A model study for Hunter L * value and drip loss
    • Hwang, I. Proteomics approach in meat science: a model study for Hunter L * value and drip loss Food Sci. Biotechnol. 2004, 13, 208-214
    • (2004) Food Sci. Biotechnol. , vol.13 , pp. 208-214
    • Hwang, I.1
  • 40
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical: An electron spin resonance investigation
    • Vasquez-Vivar, J.; Kalyanaraman, B.; Kennedy, M. C. Mitochondrial aconitase is a source of hydroxyl radical: an electron spin resonance investigation J. Biol. Chem. 2000, 275, 14064-14069
    • (2000) J. Biol. Chem. , vol.275 , pp. 14064-14069
    • Vasquez-Vivar, J.1    Kalyanaraman, B.2    Kennedy, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.