메뉴 건너뛰기




Volumn 85, Issue 4, 2010, Pages 625-631

Changed dynamics in myofibrillar protein aggregation as a consequence of heating time and temperature

Author keywords

Cooked meat; Laser granulometry; Protein aggregation

Indexed keywords

MUSCLE PROTEIN; WATER;

EID: 77954953768     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2010.03.015     Document Type: Article
Times cited : (40)

References (37)
  • 1
    • 0014262143 scopus 로고
    • Sedimentation equilibrium in reacting systems. VI. Some applications to indefinite self-association. Studies with β-lactoglobulin A
    • Adams E.T., Lewis M.S. Sedimentation equilibrium in reacting systems. VI. Some applications to indefinite self-association. Studies with β-lactoglobulin A. Biochemistry 1968, 7:1044-1053.
    • (1968) Biochemistry , vol.7 , pp. 1044-1053
    • Adams, E.T.1    Lewis, M.S.2
  • 2
    • 84893617475 scopus 로고
    • 2+-induced gelation of preheated whey protein solutions
    • 2+-induced gelation of preheated whey protein solutions. Journal of Food Science 1993, 58:867-871.
    • (1993) Journal of Food Science , vol.58 , pp. 867-871
    • Barbut, S.1    Foegeding, E.A.2
  • 3
    • 3242692878 scopus 로고    scopus 로고
    • The polyglutamine diseases
    • Oxford University Press, Oxford, G.P. Bates, P.S. Harper, L. Jones (Eds.)
    • Bates G.P., Benn C. The polyglutamine diseases. Huntington's disease 2002, 429-472. Oxford University Press, Oxford. G.P. Bates, P.S. Harper, L. Jones (Eds.).
    • (2002) Huntington's disease , pp. 429-472
    • Bates, G.P.1    Benn, C.2
  • 5
    • 33645704194 scopus 로고    scopus 로고
    • Methods for measuring protein aggregation
    • Bondos S.E. Methods for measuring protein aggregation. Current Analytical Chemistry 2006, 2:157-170.
    • (2006) Current Analytical Chemistry , vol.2 , pp. 157-170
    • Bondos, S.E.1
  • 7
    • 0017074206 scopus 로고
    • A solvent system for delipidation of plasma or serum without protein precipitation
    • Cham B.E., Knowles B.R. A solvent system for delipidation of plasma or serum without protein precipitation. Journal of Lipid Research 1976, 17:176-181.
    • (1976) Journal of Lipid Research , vol.17 , pp. 176-181
    • Cham, B.E.1    Knowles, B.R.2
  • 8
    • 33747786293 scopus 로고    scopus 로고
    • Technical note: A simplified procedure for myofibril hydrophobicity determination
    • Chelh I., Gatellier P., Santé-Lhoutellier V. Technical note: A simplified procedure for myofibril hydrophobicity determination. Meat Science 2006, 74:681-684.
    • (2006) Meat Science , vol.74 , pp. 681-684
    • Chelh, I.1    Gatellier, P.2    Santé-Lhoutellier, V.3
  • 9
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W., Przedborski S. Parkinson's disease: Mechanisms and models. Neuron 2003, 39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 10
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion disease
    • Eigen M. Prionics or the kinetic basis of prion disease. Biophysical Chemistry 1996, 63:A1-A18.
    • (1996) Biophysical Chemistry , vol.63
    • Eigen, M.1
  • 11
    • 0031693018 scopus 로고    scopus 로고
    • Evidence for impaired assimilation and increased colonic fermentation of protein related to gastric acid suppression therapy
    • Evenepoel P., Claus D., Geypens B., Maes B., Hiele M., Rutgeerts P., et al. Evidence for impaired assimilation and increased colonic fermentation of protein related to gastric acid suppression therapy. Alimentary Pharmacology and Therapeutics 1998, 12:10-11.
    • (1998) Alimentary Pharmacology and Therapeutics , vol.12 , pp. 10-11
    • Evenepoel, P.1    Claus, D.2    Geypens, B.3    Maes, B.4    Hiele, M.5    Rutgeerts, P.6
  • 12
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The connections between equilibrium and kinetic behaviour
    • Ferrone K.A. Nucleation: The connections between equilibrium and kinetic behaviour. Methods in Enzymology 2006, 412:285-299.
    • (2006) Methods in Enzymology , vol.412 , pp. 285-299
    • Ferrone, K.A.1
  • 13
    • 0030792066 scopus 로고    scopus 로고
    • Influence of dietary protein supplements on the formation of bacterial metabolites in the colon
    • Geypens B., Claus D., Evenepoel P., Hiele M., Maes B., Peeters M., et al. Influence of dietary protein supplements on the formation of bacterial metabolites in the colon. Gut 1997, 41:70-76.
    • (1997) Gut , vol.41 , pp. 70-76
    • Geypens, B.1    Claus, D.2    Evenepoel, P.3    Hiele, M.4    Maes, B.5    Peeters, M.6
  • 15
    • 85010916780 scopus 로고
    • The structure of F-actin and of actin filaments isolated from muscle
    • Hanson J., Lowy J. The structure of F-actin and of actin filaments isolated from muscle. Journal of Molecular Biology 1963, 6:46-60.
    • (1963) Journal of Molecular Biology , vol.6 , pp. 46-60
    • Hanson, J.1    Lowy, J.2
  • 16
    • 0348229449 scopus 로고    scopus 로고
    • Aggregation induced by calcium chloride and subsequent thermal gelation of whey protein isolate
    • Ju Z.Y., Kilara A. Aggregation induced by calcium chloride and subsequent thermal gelation of whey protein isolate. Journal of Dairy Science 1998, 81:925-931.
    • (1998) Journal of Dairy Science , vol.81 , pp. 925-931
    • Ju, Z.Y.1    Kilara, A.2
  • 17
    • 0012902559 scopus 로고    scopus 로고
    • Degradation of myosin by enzymes of the digestive system: Comparison between native and oxidatively cross-linked protein
    • Kamin-Belsky N., Brillon A.A., Arav R., Shaklai N. Degradation of myosin by enzymes of the digestive system: Comparison between native and oxidatively cross-linked protein. Journal of Agricultural and Food Chemistry 1996, 44:1641-1646.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 1641-1646
    • Kamin-Belsky, N.1    Brillon, A.A.2    Arav, R.3    Shaklai, N.4
  • 18
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu G., Xiong Y.L. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. Journal of Agricultural and Food Chemistry 2000, 48:624-630.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 19
    • 0028526893 scopus 로고
    • Physicochemical and function properties of protein hydrolysates in nutritional products
    • Mahmoud M.I. Physicochemical and function properties of protein hydrolysates in nutritional products. Food Technology 1994, 48:67-98.
    • (1994) Food Technology , vol.48 , pp. 67-98
    • Mahmoud, M.I.1
  • 20
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris A.M., Watzky M.A., Finke R.G. Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. Biochimica et Biophysica Acta 2009, 1794:375-397.
    • (2009) Biochimica et Biophysica Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 21
    • 21844501512 scopus 로고
    • Structural and mechanical changes in raw and cooked single porcine muscle fibres extended to fracture
    • Mutungi G., Purslow P., Warkup C. Structural and mechanical changes in raw and cooked single porcine muscle fibres extended to fracture. Meat Science 1995, 40:217-234.
    • (1995) Meat Science , vol.40 , pp. 217-234
    • Mutungi, G.1    Purslow, P.2    Warkup, C.3
  • 25
    • 0033481199 scopus 로고    scopus 로고
    • Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosous during heating
    • Palka K., Daun H. Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosous during heating. Meat Science 1999, 51:237-243.
    • (1999) Meat Science , vol.51 , pp. 237-243
    • Palka, K.1    Daun, H.2
  • 26
    • 0034386409 scopus 로고    scopus 로고
    • Effect of peptide distribution on the fractionation of whey protein hydrolysates by nanofiltration membranes
    • Pouliot Y., Gauthier S.F., l'Heureux J. Effect of peptide distribution on the fractionation of whey protein hydrolysates by nanofiltration membranes. Lait 2000, 80:113-122.
    • (2000) Lait , vol.80 , pp. 113-122
    • Pouliot, Y.1    Gauthier, S.F.2    l'Heureux, J.3
  • 29
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S.B. Molecular biology of prion diseases. Science 1991, 252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 30
    • 0014957783 scopus 로고
    • Molecular weights, association and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations
    • Reisler E., Pouyet J., Eisenberg H. Molecular weights, association and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations. Biochemistry 1970, 9:3095-3102.
    • (1970) Biochemistry , vol.9 , pp. 3095-3102
    • Reisler, E.1    Pouyet, J.2    Eisenberg, H.3
  • 33
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity; new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity; new insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine 2003, 81:678-699.
    • (2003) Journal of Molecular Medicine , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 34
    • 33846491812 scopus 로고    scopus 로고
    • Aging-induced changes in microstructure and water distribution in fresh and cooked pork in relation to water holding capacity and cooking loss - A combined confocal laser scanning microscopy (CLSM) and low-field nuclear magnetic resonance relaxation study
    • Straadt I., Rasmussen M., Andersen H.J., Bertram H.C. Aging-induced changes in microstructure and water distribution in fresh and cooked pork in relation to water holding capacity and cooking loss - A combined confocal laser scanning microscopy (CLSM) and low-field nuclear magnetic resonance relaxation study. Meat Science 2007, 75:687-695.
    • (2007) Meat Science , vol.75 , pp. 687-695
    • Straadt, I.1    Rasmussen, M.2    Andersen, H.J.3    Bertram, H.C.4
  • 35
    • 0030503837 scopus 로고    scopus 로고
    • Effect of postrigor sarcomere length on mechanical and structural characteristics of raw and heat-denatured single pork muscle fibers
    • Willems M.E.T., Purslow P.P. Effect of postrigor sarcomere length on mechanical and structural characteristics of raw and heat-denatured single pork muscle fibers. Journal of Texture Studies 1996, 27:217-233.
    • (1996) Journal of Texture Studies , vol.27 , pp. 217-233
    • Willems, M.E.T.1    Purslow, P.P.2
  • 36
    • 0018930034 scopus 로고
    • Structure of collagen fibril: Some variations on theme of tetragonally packed dimmers
    • Woodhead-Galloway J. Structure of collagen fibril: Some variations on theme of tetragonally packed dimmers. Proceedings of the Royal Society, London, B 1980, 209:275-297.
    • (1980) Proceedings of the Royal Society, London, B , vol.209 , pp. 275-297
    • Woodhead-Galloway, J.1
  • 37
    • 0041386023 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of threadfin bream actomyosin
    • Yongsawatdigul J., Park J.W. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry 2003, 83:409-416.
    • (2003) Food Chemistry , vol.83 , pp. 409-416
    • Yongsawatdigul, J.1    Park, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.