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Volumn 88, Issue 2, 2011, Pages 234-240

Comparative study on the stability of fish actomyosin and pork actomyosin

Author keywords

Actomyosin; Ionic strength; PH; Stability; Temperature

Indexed keywords

ACTOMYOSIN; COMPARATIVE STUDIES; CONTENT MEASUREMENTS; DISULFIDE BONDS; EFFECTS OF TEMPERATURE; PH CHANGE; SULFHYDRYL GROUPS; UV SPECTRUM;

EID: 79951772079     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2010.12.026     Document Type: Article
Times cited : (48)

References (30)
  • 1
    • 62349141549 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef
    • Ahhmed A.M., Nasu T., Huy D.Q., Tomisaka Y., Kawahara S., Muguruma M. Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef. Meat Science 2009, 82:170-178.
    • (2009) Meat Science , vol.82 , pp. 170-178
    • Ahhmed, A.M.1    Nasu, T.2    Huy, D.Q.3    Tomisaka, Y.4    Kawahara, S.5    Muguruma, M.6
  • 2
    • 2942545081 scopus 로고    scopus 로고
    • Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish
    • Benjakul S., Visessanguan W., Chantarasuwan C. Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish. Journal of Food Science and Technology 2004, 39:671-680.
    • (2004) Journal of Food Science and Technology , vol.39 , pp. 671-680
    • Benjakul, S.1    Visessanguan, W.2    Chantarasuwan, C.3
  • 3
    • 2942687864 scopus 로고    scopus 로고
    • Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment-A low-field NMR study
    • Bertram H.C., Kristensen M., Andersen H.J. Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment-A low-field NMR study. Meat Science 2004, 68:249-256.
    • (2004) Meat Science , vol.68 , pp. 249-256
    • Bertram, H.C.1    Kristensen, M.2    Andersen, H.J.3
  • 4
    • 51249086410 scopus 로고    scopus 로고
    • Characterization of fish myosin aggregates using static and dynamic light scattering
    • Brenner T., Johannsson R., Nicolai T. Characterization of fish myosin aggregates using static and dynamic light scattering. Food Hydrocolloids 2009, 23:296-305.
    • (2009) Food Hydrocolloids , vol.23 , pp. 296-305
    • Brenner, T.1    Johannsson, R.2    Nicolai, T.3
  • 5
    • 84987297811 scopus 로고
    • Cross-linking of myosin heave chains from cod, herring and silver hake during thermal setting
    • Chan J.K., Gill T.A., Paulson A.T. Cross-linking of myosin heave chains from cod, herring and silver hake during thermal setting. Journal of Food Science 1992, 57:906-912.
    • (1992) Journal of Food Science , vol.57 , pp. 906-912
    • Chan, J.K.1    Gill, T.A.2    Paulson, A.T.3
  • 7
    • 0001140138 scopus 로고
    • Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels
    • Foegeding E.A., Allen C.E., Dayton W.R. Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. Journal of Food Science 1986, 51(1):104-108.
    • (1986) Journal of Food Science , vol.51 , Issue.1 , pp. 104-108
    • Foegeding, E.A.1    Allen, C.E.2    Dayton, W.R.3
  • 8
    • 0002832945 scopus 로고
    • Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin
    • Gill T.A., Chan J.K., Paulson A.T. Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin. Food Research International 1992, 25:333-341.
    • (1992) Food Research International , vol.25 , pp. 333-341
    • Gill, T.A.1    Chan, J.K.2    Paulson, A.T.3
  • 9
    • 51749125660 scopus 로고    scopus 로고
    • Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases
    • Hemung B.O., Li-Chan E.C.Y., Yongsawatdigul J. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chemistry 2008, 111:439-446.
    • (2008) Food Chemistry , vol.111 , pp. 439-446
    • Hemung, B.O.1    Li-Chan, E.C.Y.2    Yongsawatdigul, J.3
  • 10
    • 0018322291 scopus 로고
    • Aggregation and denaturation involved in gel formation
    • American Chemical Society, Washington, DC, A. Pour-El (Ed.)
    • Hermansson A.M. Aggregation and denaturation involved in gel formation. Functionality and protein structure 1979, 81-103. American Chemical Society, Washington, DC. A. Pour-El (Ed.).
    • (1979) Functionality and protein structure , pp. 81-103
    • Hermansson, A.M.1
  • 11
    • 0035545569 scopus 로고    scopus 로고
    • The relationship between tenderness, proteolysis, muscle contraction and dissociation of actomyosin
    • Hopkins D.L., Thompson J.M. The relationship between tenderness, proteolysis, muscle contraction and dissociation of actomyosin. Meat Science 2001, 57:1-12.
    • (2001) Meat Science , vol.57 , pp. 1-12
    • Hopkins, D.L.1    Thompson, J.M.2
  • 12
    • 33846967090 scopus 로고    scopus 로고
    • Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Orechromis niloticus) on hydrostatic pressure treatment
    • Hsu K.C., Hwang J.S., Yu C.C., Jao C.L. Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Orechromis niloticus) on hydrostatic pressure treatment. Food Chemistry 2007, 103:560-564.
    • (2007) Food Chemistry , vol.103 , pp. 560-564
    • Hsu, K.C.1    Hwang, J.S.2    Yu, C.C.3    Jao, C.L.4
  • 13
    • 34248394702 scopus 로고    scopus 로고
    • Contribution of hydrophobicity, net charge, and sulfhydryl groups to thermal properties of ovalbumin
    • Ko W.C., Yu C.C., Hsu K.C. Contribution of hydrophobicity, net charge, and sulfhydryl groups to thermal properties of ovalbumin. LWT Food Science and Technology 2007, 40:1316-1320.
    • (2007) LWT Food Science and Technology , vol.40 , pp. 1316-1320
    • Ko, W.C.1    Yu, C.C.2    Hsu, K.C.3
  • 14
    • 33746375397 scopus 로고    scopus 로고
    • Effect of pH-shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins
    • Kristinsson H.G., Liang Y. Effect of pH-shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins. Journal of Food Science 2006, 71(5):C304-C312.
    • (2006) Journal of Food Science , vol.71 , Issue.5
    • Kristinsson, H.G.1    Liang, Y.2
  • 16
    • 0036129584 scopus 로고    scopus 로고
    • Thermal gelation of brown trout myofibrils from white and red muscles: Effect of pH and ionic strength
    • Lefèvre F., Fauconneau B., Ouali A., Culioli J. Thermal gelation of brown trout myofibrils from white and red muscles: Effect of pH and ionic strength. Journal of the Science of Food and Agriculture 2002, 82(4):452-463.
    • (2002) Journal of the Science of Food and Agriculture , vol.82 , Issue.4 , pp. 452-463
    • Lefèvre, F.1    Fauconneau, B.2    Ouali, A.3    Culioli, J.4
  • 17
    • 7444258535 scopus 로고    scopus 로고
    • The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash
    • Lin S.B., Chen L.C., Chen H.H. The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash. Food Research International 2005, 38:19-27.
    • (2005) Food Research International , vol.38 , pp. 19-27
    • Lin, S.B.1    Chen, L.C.2    Chen, H.H.3
  • 19
    • 34548490104 scopus 로고    scopus 로고
    • Studies on fish and pork paste gelation by dynamic rheology and circular dichroism
    • Liu R., Zhao S.M., Xiong S.B., Xie B.J., Liu H.M. Studies on fish and pork paste gelation by dynamic rheology and circular dichroism. Journal of Food Science 2007, 72:E399-E403.
    • (2007) Journal of Food Science , vol.72
    • Liu, R.1    Zhao, S.M.2    Xiong, S.B.3    Xie, B.J.4    Liu, H.M.5
  • 20
    • 50249126674 scopus 로고    scopus 로고
    • Role of secondary structures in the gelation of porcine myosin at different pH values
    • Liu R., Zhao S.M., Xiong S.B., Xie B.J., Qin L.H. Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science 2008, 80:632-639.
    • (2008) Meat Science , vol.80 , pp. 632-639
    • Liu, R.1    Zhao, S.M.2    Xiong, S.B.3    Xie, B.J.4    Qin, L.H.5
  • 23
    • 33748762209 scopus 로고    scopus 로고
    • Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization
    • Pérez-Mateos M., Lanier T.C. Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization. Food Chemistry 2006, 101:1223-1229.
    • (2006) Food Chemistry , vol.101 , pp. 1223-1229
    • Pérez-Mateos, M.1    Lanier, T.C.2
  • 24
    • 35448952867 scopus 로고    scopus 로고
    • Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding
    • Raghavan S., Kristinsson H.G. Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding. Food Chemistry 2008, 107:385-398.
    • (2008) Food Chemistry , vol.107 , pp. 385-398
    • Raghavan, S.1    Kristinsson, H.G.2
  • 25
    • 39149097500 scopus 로고    scopus 로고
    • Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota)
    • Riebroy S., Benjakul S., Visessanguan W., Erikson U., Rustad T. Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota). Food Chemistry 2008, 109:42-53.
    • (2008) Food Chemistry , vol.109 , pp. 42-53
    • Riebroy, S.1    Benjakul, S.2    Visessanguan, W.3    Erikson, U.4    Rustad, T.5
  • 26
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of Arrowtooth Flounder myosin
    • Visessanguan W., Ogawa M., Nakai S., An H. Physicochemical changes and mechanism of heat-induced gelation of Arrowtooth Flounder myosin. Journal of Agricultural and Food Chemistry 2000, 48:1016-1023.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4
  • 27
    • 15344340163 scopus 로고    scopus 로고
    • Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation
    • Westphalen A.D., Briggs J.L., Lonergan S.M. Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation. Meat Science 2005, 70:293-299.
    • (2005) Meat Science , vol.70 , pp. 293-299
    • Westphalen, A.D.1    Briggs, J.L.2    Lonergan, S.M.3
  • 28
    • 67349122272 scopus 로고    scopus 로고
    • Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish (Mulloidichthys martinicus) muscle as influenced by iced storage
    • Yarnpakdee S., Benjakul S., Visessanguan W., Kijroongrojana K. Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish (Mulloidichthys martinicus) muscle as influenced by iced storage. Food Hydrocolloids 2009, 23:1779-1784.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1779-1784
    • Yarnpakdee, S.1    Benjakul, S.2    Visessanguan, W.3    Kijroongrojana, K.4
  • 29
    • 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
  • 30
    • 33750937422 scopus 로고    scopus 로고
    • Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting
    • Yongsawatdigul J., Sinsuwan S. Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting. Food Hydrocolloids 2007, 21:359-367.
    • (2007) Food Hydrocolloids , vol.21 , pp. 359-367
    • Yongsawatdigul, J.1    Sinsuwan, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.