메뉴 건너뛰기




Volumn 83, Issue 2, 2009, Pages 239-245

Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles

Author keywords

Freeze thaw cycles; Physicochemical property; Pork; Protein oxidation

Indexed keywords

SUS;

EID: 67649850393     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.05.003     Document Type: Article
Times cited : (437)

References (51)
  • 2
    • 0004202155 scopus 로고
    • Association of the Official Analytical Chemists, Washington, DC
    • AOAC. Official method of analysis. 16th ed. (1995), Association of the Official Analytical Chemists, Washington, DC
    • (1995) Official method of analysis. 16th ed.
    • AOAC1
  • 3
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • Benjakul S., Seymour T.S., Morrissey M.T., and An H. Physicochemical changes in Pacific whiting muscle proteins during iced storage. Journal of Food Science 62 (1997) 729-733
    • (1997) Journal of Food Science , vol.62 , pp. 729-733
    • Benjakul, S.1    Seymour, T.S.2    Morrissey, M.T.3    An, H.4
  • 4
    • 0042427804 scopus 로고    scopus 로고
    • Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage
    • Benjakul S., Visessanguan W., Thongkaew C., and Tanaka M. Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International 36 (2003) 787-795
    • (2003) Food Research International , vol.36 , pp. 787-795
    • Benjakul, S.1    Visessanguan, W.2    Thongkaew, C.3    Tanaka, M.4
  • 5
    • 33750962919 scopus 로고    scopus 로고
    • Effects of freezing and thawing on the quality changes of tiger shrimp (Penaeus monodon) frozen by air-blast and cryogenic freezing
    • Boonsumrej S., Chaiwanichsiri S., Tantratian S., Suzuki T., and Takai R. Effects of freezing and thawing on the quality changes of tiger shrimp (Penaeus monodon) frozen by air-blast and cryogenic freezing. Journal of Food Engineering 80 (2007) 292-299
    • (2007) Journal of Food Engineering , vol.80 , pp. 292-299
    • Boonsumrej, S.1    Chaiwanichsiri, S.2    Tantratian, S.3    Suzuki, T.4    Takai, R.5
  • 6
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies K.J. Degradation of oxidized proteins by the 20S proteasome. Biochimie 83 (2001) 301-310
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 7
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochemical Journal 324 (1997) 1-18
    • (1997) Biochemical Journal , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 8
    • 84988164324 scopus 로고
    • Effect of frozen storage on the chemical and physical properties of black and silver scabbard fish
    • Dias J., Nunes M.L., and Mendes R. Effect of frozen storage on the chemical and physical properties of black and silver scabbard fish. Journal of the Science of Food and Agriculture 66 (1994) 327-335
    • (1994) Journal of the Science of Food and Agriculture , vol.66 , pp. 327-335
    • Dias, J.1    Nunes, M.L.2    Mendes, R.3
  • 9
    • 0030176664 scopus 로고    scopus 로고
    • Calpains from thaw rigor muscle
    • Dransfield E. Calpains from thaw rigor muscle. Meat Science 43 (1996) 311-320
    • (1996) Meat Science , vol.43 , pp. 311-320
    • Dransfield, E.1
  • 12
    • 1842334976 scopus 로고
    • Frozen storage stability of whole and headless freshwater prawns, Machrobranchium rosenbergii
    • Hale M.B., and Waters M.E. Frozen storage stability of whole and headless freshwater prawns, Machrobranchium rosenbergii. Marine Fish Review 42 (1981) 18-21
    • (1981) Marine Fish Review , vol.42 , pp. 18-21
    • Hale, M.B.1    Waters, M.E.2
  • 13
    • 0006814424 scopus 로고
    • Delocalization of mitochondrial enzymes during freezing and thawing of skeletal muscle
    • Fennema O.R. (Ed), American Chemical Society, Washington, DC
    • Hamm R. Delocalization of mitochondrial enzymes during freezing and thawing of skeletal muscle. In: Fennema O.R. (Ed). Proteins at low temperatures. Advances in chemistry series Vol. 180 (1979), American Chemical Society, Washington, DC 191
    • (1979) Proteins at low temperatures. Advances in chemistry series , vol.180 , pp. 191
    • Hamm, R.1
  • 14
    • 0034819490 scopus 로고    scopus 로고
    • Elucidation of protein-lipid interactions in lysozyme-corn oil system by Fourier transform Raman spectroscopy
    • Howell N.K., Herman H., and Li-Chan E.C.Y. Elucidation of protein-lipid interactions in lysozyme-corn oil system by Fourier transform Raman spectroscopy. Journal of Agricultural and Food Chemistry 49 (2001) 1529-1533
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 1529-1533
    • Howell, N.K.1    Herman, H.2    Li-Chan, E.C.Y.3
  • 15
    • 22144487389 scopus 로고    scopus 로고
    • Mechanisms of water-holding capacity of meat: Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes
    • Huff-Lonergan E., and Lonergan S.M. Mechanisms of water-holding capacity of meat: Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Science 71 (2005) 194-204
    • (2005) Meat Science , vol.71 , pp. 194-204
    • Huff-Lonergan, E.1    Lonergan, S.M.2
  • 16
  • 17
    • 0000372510 scopus 로고
    • Properties of actin and stability of the actomyosin reconstituted from milkfish (Chanos chanos) actin and myosin
    • Jiang S.T., Wang F.J., and Chen C.S. Properties of actin and stability of the actomyosin reconstituted from milkfish (Chanos chanos) actin and myosin. Journal of Agriculture and Food Chemistry 37 (1989) 1232-1235
    • (1989) Journal of Agriculture and Food Chemistry , vol.37 , pp. 1232-1235
    • Jiang, S.T.1    Wang, F.J.2    Chen, C.S.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0001475995 scopus 로고    scopus 로고
    • Lipid oxidation and myosin denaturation in dark chicken meat
    • Li S.J., and King A.J. Lipid oxidation and myosin denaturation in dark chicken meat. Journal of Agricultural and Food Chemistry 44 (1996) 3080-3084
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 3080-3084
    • Li, S.J.1    King, A.J.2
  • 21
    • 0033827809 scopus 로고    scopus 로고
    • Chemical, physical, and gel-forming properties of oxidized myofibrils and whey-and soy-protein isolates
    • Liu G., Xiong Y.L., and Butterfield D.A. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey-and soy-protein isolates. Journal of Food Science 65 5 (2000) 811-818
    • (2000) Journal of Food Science , vol.65 , Issue.5 , pp. 811-818
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 22
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu G., and Xiong Y.L. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. Journal of Agricultural and Food Chemistry 48 (2000) 624-630
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 23
    • 0000584434 scopus 로고    scopus 로고
    • Contribution of lipid and protein oxidation to rheological differences between chicken white and red muscle myofibrillar proteins
    • Liu G., and Xiong Y.L. Contribution of lipid and protein oxidation to rheological differences between chicken white and red muscle myofibrillar proteins. Journal of Agricultural and Food Chemistry 44 (1996) 779-784
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 779-784
    • Liu, G.1    Xiong, Y.L.2
  • 24
    • 33847103240 scopus 로고    scopus 로고
    • The combined effect of antioxidants and modified atmosphere packaging on protein and lipid oxidation in beef patties during chill storage
    • Lund M.N., Hviid M.S., and Skibsted L.H. The combined effect of antioxidants and modified atmosphere packaging on protein and lipid oxidation in beef patties during chill storage. Meat Science 76 (2007) 226-233
    • (2007) Meat Science , vol.76 , pp. 226-233
    • Lund, M.N.1    Hviid, M.S.2    Skibsted, L.H.3
  • 25
    • 33646525423 scopus 로고    scopus 로고
    • Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins
    • Morzel M., Gatellier P., Sayd T., Renerre M., and Laville E. Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins. Meat Science 73 (2006) 536-543
    • (2006) Meat Science , vol.73 , pp. 536-543
    • Morzel, M.1    Gatellier, P.2    Sayd, T.3    Renerre, M.4    Laville, E.5
  • 27
    • 34548226860 scopus 로고    scopus 로고
    • Hydroxyl radical oxidation destabilizes subfragment-1 but not the rod of myosin in chicken myofibrils
    • Ooizumi T., and Xiong Y.L. Hydroxyl radical oxidation destabilizes subfragment-1 but not the rod of myosin in chicken myofibrils. Food Chemistry 106 (2008) 661-668
    • (2008) Food Chemistry , vol.106 , pp. 661-668
    • Ooizumi, T.1    Xiong, Y.L.2
  • 28
    • 0001610709 scopus 로고
    • Effect of muscle lysosomal enzymes and calcium activated neutral proteinase on myofibriallar ATPase activity: Relationship with aging changes
    • Ouali A., and Valin C. Effect of muscle lysosomal enzymes and calcium activated neutral proteinase on myofibriallar ATPase activity: Relationship with aging changes. Meat Science 5 (1981) 233-245
    • (1981) Meat Science , vol.5 , pp. 233-245
    • Ouali, A.1    Valin, C.2
  • 29
    • 84986533545 scopus 로고
    • Biochemical and morphological changes in grass shrimp (Penaeus monodon) muscle following freezing by air blast and liquid nitrogen methods
    • Pan B.S., and Yeh W.T. Biochemical and morphological changes in grass shrimp (Penaeus monodon) muscle following freezing by air blast and liquid nitrogen methods. Journal of Food Biochemistry 17 (1993) 147-160
    • (1993) Journal of Food Biochemistry , vol.17 , pp. 147-160
    • Pan, B.S.1    Yeh, W.T.2
  • 30
    • 33745757012 scopus 로고    scopus 로고
    • Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems
    • Park D., Xiong Y.L., Alderton A.L., and Ooizumi. Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems. Journal of Agricultural and Food Chemistry 54 (2006) 4445-4451
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 4445-4451
    • Park, D.1    Xiong, Y.L.2    Alderton, A.L.3    Ooizumi4
  • 31
    • 0017342054 scopus 로고    scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Porzio M.A., and Pearson A.M. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochimica et Biophysica Acta 490 (1997) 27-34
    • (1997) Biochimica et Biophysica Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 32
    • 84985233003 scopus 로고
    • Changes in electrophoretic patterns of gadoid and non-gadoid fish muscle during frozen storage
    • Ragnarsson K., and Regenstein J.M. Changes in electrophoretic patterns of gadoid and non-gadoid fish muscle during frozen storage. Journal of Food Science 54 4 (1989) 819-823
    • (1989) Journal of Food Science , vol.54 , Issue.4 , pp. 819-823
    • Ragnarsson, K.1    Regenstein, J.M.2
  • 34
    • 3042529321 scopus 로고
    • Effect of ATP on the binding of N-ethylmaleimide to SH groups in the active site of myosin ATPase
    • Sekine T., and Yamaguchi M. Effect of ATP on the binding of N-ethylmaleimide to SH groups in the active site of myosin ATPase. Journal of Biochemistry 54 (1963) 196-208
    • (1963) Journal of Biochemistry , vol.54 , pp. 196-208
    • Sekine, T.1    Yamaguchi, M.2
  • 35
    • 0000665651 scopus 로고
    • Theories of protein denaturation during frozen storage of fish flesh
    • Shenouda S.Y.K. Theories of protein denaturation during frozen storage of fish flesh. Advances in Food Research 26 (1980) 275-311
    • (1980) Advances in Food Research , vol.26 , pp. 275-311
    • Shenouda, S.Y.K.1
  • 36
    • 0000361142 scopus 로고
    • The 2-thiobarbituric acid reaction, an objective measure of the oxidative deterioration occurring in fats and oils
    • Sinnhuber R.O., and Yu T.C. The 2-thiobarbituric acid reaction, an objective measure of the oxidative deterioration occurring in fats and oils. Journal of Japan Oil Chemists' Society 25 (1977) 259-267
    • (1977) Journal of Japan Oil Chemists' Society , vol.25 , pp. 259-267
    • Sinnhuber, R.O.1    Yu, T.C.2
  • 37
    • 0035179693 scopus 로고    scopus 로고
    • Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cycles
    • Soottawat B., and Friedrich B. Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cycles. Food Chemistry 72 (2001) 207-217
    • (2001) Food Chemistry , vol.72 , pp. 207-217
    • Soottawat, B.1    Friedrich, B.2
  • 38
    • 34247157176 scopus 로고    scopus 로고
    • Comparative studies on the effect of the freeze-thawing process on the physicochemical properties and microstructures of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) muscle
    • Sriket P., Benjakul S., and Visessanguan W. Comparative studies on the effect of the freeze-thawing process on the physicochemical properties and microstructures of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) muscle. Food Chemistry 104 (2007) 113-121
    • (2007) Food Chemistry , vol.104 , pp. 113-121
    • Sriket, P.1    Benjakul, S.2    Visessanguan, W.3
  • 39
    • 0030863688 scopus 로고    scopus 로고
    • Effects of freezing and thawing methods and storage time on thermal properties of freshwater prawns (Macrobrachium rosenbergii)
    • Srinivasan S., Xiong Y.L., and Blanchard S.P. Effects of freezing and thawing methods and storage time on thermal properties of freshwater prawns (Macrobrachium rosenbergii). Journal of Science and Food Agriculture 75 (1997) 37-44
    • (1997) Journal of Science and Food Agriculture , vol.75 , pp. 37-44
    • Srinivasan, S.1    Xiong, Y.L.2    Blanchard, S.P.3
  • 40
    • 0030829476 scopus 로고    scopus 로고
    • Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze-thaw cycles
    • Srinivasan S., Xiong Y.L., Blanchard S.P., and Tidwell J.H. Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze-thaw cycles. Journal of Food Science 62 (1997) 123-127
    • (1997) Journal of Food Science , vol.62 , pp. 123-127
    • Srinivasan, S.1    Xiong, Y.L.2    Blanchard, S.P.3    Tidwell, J.H.4
  • 41
    • 0025674536 scopus 로고
    • Metal ion-catalysed oxidation of proteins: biochemical mechanism and biological consequences
    • Stadtman E.R. Metal ion-catalysed oxidation of proteins: biochemical mechanism and biological consequences. Free Radical Biology and Medicine 8 (1990) 315-325
    • (1990) Free Radical Biology and Medicine , vol.8 , pp. 315-325
    • Stadtman, E.R.1
  • 42
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acids residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acids residues in proteins by radiolysis and by metal-catalyzed reactions. Annual Review of Biochemistry 62 (1993) 797-821
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 43
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., and Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chemical Research in Toxicology 10 (1997) 485-494
    • (1997) Chemical Research in Toxicology , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 44
    • 26444443445 scopus 로고    scopus 로고
    • The effect of metal ions on lipid oxidation, color and physicochemical properties of cuttlefish (Sepia pharaoni) subjected to multiple freeze-thaw cycles
    • Thanonkaew A., Benjakul S., and Visessanguan W. The effect of metal ions on lipid oxidation, color and physicochemical properties of cuttlefish (Sepia pharaoni) subjected to multiple freeze-thaw cycles. Food Chemistry 95 (2006) 591-599
    • (2006) Food Chemistry , vol.95 , pp. 591-599
    • Thanonkaew, A.1    Benjakul, S.2    Visessanguan, W.3
  • 45
    • 85005658287 scopus 로고
    • Effect of freezing rate on the denaturation of myofibrillar proteins
    • Wagner J.R., and Anon. Effect of freezing rate on the denaturation of myofibrillar proteins. International Journal of Food Science and Technology 20 (1985) 735-744
    • (1985) International Journal of Food Science and Technology , vol.20 , pp. 735-744
    • Wagner, J.R.1
  • 46
    • 85005583458 scopus 로고
    • Effect of frozen storage on protein denaturation in bovine muscle1. Myofibrillar ATPase activity and differential scanning calorimetric studies
    • Wagner J.R., and Anon. Effect of frozen storage on protein denaturation in bovine muscle1. Myofibrillar ATPase activity and differential scanning calorimetric studies. International Journal of Food Science and Technology 21 (1986) 9-18
    • (1986) International Journal of Food Science and Technology , vol.21 , pp. 9-18
    • Wagner, J.R.1
  • 47
    • 28444440308 scopus 로고    scopus 로고
    • Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability
    • Wang L.L., and Xiong Y.L. Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability. Journal of Agriculture and Food Chemistry 53 (2005) 9186-9192
    • (2005) Journal of Agriculture and Food Chemistry , vol.53 , pp. 9186-9192
    • Wang, L.L.1    Xiong, Y.L.2
  • 48
    • 0018805375 scopus 로고
    • Inactivation of myosin subfragment one by cobalt(II)/cobalt(III) phenanthroline complexes 2. Cobalt chelation of two critical SH groups
    • Wells J.A., Werber M.M., and Yount R.G. Inactivation of myosin subfragment one by cobalt(II)/cobalt(III) phenanthroline complexes 2. Cobalt chelation of two critical SH groups. Biochemistry 18 (1979) 4800-4805
    • (1979) Biochemistry , vol.18 , pp. 4800-4805
    • Wells, J.A.1    Werber, M.M.2    Yount, R.G.3
  • 49
    • 0030895919 scopus 로고    scopus 로고
    • Modification of muscle protein functionality by antioxidants
    • Damodaran S. (Ed), Plenum Press, New York
    • Xiong Y.L., Sirinivasan S., and Liu G. Modification of muscle protein functionality by antioxidants. In: Damodaran S. (Ed). Food proteins and lipids (1997), Plenum Press, New York 95-108
    • (1997) Food proteins and lipids , pp. 95-108
    • Xiong, Y.L.1    Sirinivasan, S.2    Liu, G.3
  • 50
    • 0242396711 scopus 로고    scopus 로고
    • Protein oxidation and implication for muscle food quality
    • Decker E.A., Faustman C.L., and Lopez-Bote C.J. (Eds), John Wiley and Sons Inc., New York
    • Xiong Y.L. Protein oxidation and implication for muscle food quality. In: Decker E.A., Faustman C.L., and Lopez-Bote C.J. (Eds). Antioxidants in muscle foods (2000), John Wiley and Sons Inc., New York 85-111
    • (2000) Antioxidants in muscle foods , pp. 85-111
    • Xiong, Y.L.1
  • 51
    • 22944451801 scopus 로고    scopus 로고
    • Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles
    • Yu L.H., Lee E.S., and Jong J.Y. Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles. Meat Science 71 (2005) 375-382
    • (2005) Meat Science , vol.71 , pp. 375-382
    • Yu, L.H.1    Lee, E.S.2    Jong, J.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.