메뉴 건너뛰기




Volumn 78, Issue 7, 2013, Pages

Rapid heating of Alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties

Author keywords

Gelation; Isothermal heating; Myofibrillar protein; Species; Viscoelasticity

Indexed keywords

FISH PROTEIN; MUSCLE PROTEIN; MYOSIN;

EID: 84880601395     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/1750-3841.12147     Document Type: Article
Times cited : (17)

References (36)
  • 2
    • 84987341379 scopus 로고
    • Influence of poultry species, muscle groups, and NaCl level on strength, deformability, and water retention in heat-set muscle gels
    • Amato PM, Hamann DD, Ball HR, Foegeding EA. 1989. Influence of poultry species, muscle groups, and NaCl level on strength, deformability, and water retention in heat-set muscle gels. J Food Sci 54(5):1136-40.
    • (1989) J Food Sci , vol.54 , Issue.5 , pp. 1136-1140
    • Amato, P.M.1    Hamann, D.D.2    Ball, H.R.3    Foegeding, E.A.4
  • 3
    • 84880596346 scopus 로고    scopus 로고
    • AOAC International. Meat and meat products. In: Cunniff P, editor. 16th ed. Chapter 39. Gaithersburg, MD: AOAC International
    • AOAC International. 1996. Meat and meat products. In: Cunniff P, editor. Official methods of analysis of AOAC International. 16th ed. Chapter 39. Gaithersburg, MD: AOAC International. p 1-6.
    • (1996) Official methods of analysis of AOAC International , pp. 1-6
  • 4
    • 0021131036 scopus 로고
    • Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress
    • Asghar A, Morita J, Samejima K, Yasui T. 1984. Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agric Biol Chem 48(9):2217-24.
    • (1984) Agric Biol Chem , vol.48 , Issue.9 , pp. 2217-2224
    • Asghar, A.1    Morita, J.2    Samejima, K.3    Yasui, T.4
  • 5
    • 84985219442 scopus 로고
    • Effect of heating rate and protein-concentration on gel strength and water-loss of muscle protein gels
    • Camou JP, Sebranek JG, Olson DG. 1989. Effect of heating rate and protein-concentration on gel strength and water-loss of muscle protein gels. J Food Sci 54(4):850-4.
    • (1989) J Food Sci , vol.54 , Issue.4 , pp. 850-854
    • Camou, J.P.1    Sebranek, J.G.2    Olson, D.G.3
  • 6
    • 73949142201 scopus 로고    scopus 로고
    • Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle
    • Choi YM, Lee SH, Choe JH, Rhee MS, Lee SK, Joo ST, Kim BC. 2010. Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle. Livestock Sci 127(2-3):183-91.
    • (2010) Livestock Sci , vol.127 , Issue.2-3 , pp. 183-191
    • Choi, Y.M.1    Lee, S.H.2    Choe, J.H.3    Rhee, M.S.4    Lee, S.K.5    Joo, S.T.6    Kim, B.C.7
  • 7
    • 0005969113 scopus 로고
    • Myosins from red and white bovine muscles - differences measured by turbidimetric, calorimetric and rheological techniques
    • Egelandsdal B, Martinsen BK, Fretheim K, Pettersen M, Harbitz O. 1994. Myosins from red and white bovine muscles - differences measured by turbidimetric, calorimetric and rheological techniques. J Sci Food Agric 64(1):75-85.
    • (1994) J Sci Food Agric , vol.64 , Issue.1 , pp. 75-85
    • Egelandsdal, B.1    Martinsen, B.K.2    Fretheim, K.3    Pettersen, M.4    Harbitz, O.5
  • 8
    • 84880619387 scopus 로고    scopus 로고
    • C- and H-proteins
    • In: Kreis T, Vale R, editors. 2nd ed. Oxford: Oxford University Press.
    • Fischman D, Reinach F. 1999. C- and H-proteins. In: Kreis T, Vale R, editors. Guidebook to the cytoskeletal and motor proteins. 2nd ed. Oxford: Oxford University Press. p 467-70.
    • (1999) Guidebook to the cytoskeletal and motor proteins , pp. 467-470
    • Fischman, D.1    Reinach, F.2
  • 9
    • 0001140138 scopus 로고
    • Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels
    • Foegeding EA, Allen CE, Dayton WR. 1986. Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. J Food Sci 51(1):104-9.
    • (1986) J Food Sci , vol.51 , Issue.1 , pp. 104-109
    • Foegeding, E.A.1    Allen, C.E.2    Dayton, W.R.3
  • 10
    • 0023018968 scopus 로고
    • Myosins from red and white bovine muscles. 1. Gel strength (elasticity) and water-holding capacity of heat-induced gels
    • Fretheim K, Samejima K, Egelandsdal B. 1986. Myosins from red and white bovine muscles. 1. Gel strength (elasticity) and water-holding capacity of heat-induced gels. Food Chem 22(2):107-21.
    • (1986) Food Chem , vol.22 , Issue.2 , pp. 107-121
    • Fretheim, K.1    Samejima, K.2    Egelandsdal, B.3
  • 11
    • 84987350929 scopus 로고
    • Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg-white
    • Hamann DD, Amato PM, Wu MC, Foegeding EA. 1990. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg-white. J Food Sci 55(3):665-9.
    • (1990) J Food Sci , vol.55 , Issue.3 , pp. 665-669
    • Hamann, D.D.1    Amato, P.M.2    Wu, M.C.3    Foegeding, E.A.4
  • 12
    • 0001349832 scopus 로고
    • Instrumental methods for predicting seafood sensory texture quality
    • In: Kramer DE, Liston J, editors. Barking, U.K.: Elsevier.
    • Hamann DD, Lanier TC. 1987. Instrumental methods for predicting seafood sensory texture quality. In: Kramer DE, Liston J, editors. Seafood quality determination. Barking, U.K.: Elsevier. p 123-36.
    • (1987) Seafood quality determination , pp. 123-136
    • Hamann, D.D.1    Lanier, T.C.2
  • 13
    • 84985262185 scopus 로고
    • Fracture of Alaska pollock gels in water - effects of minced muscle processing and test temperature
    • Howe J, Hamann D, Lanier T, Park J. 1994. Fracture of Alaska pollock gels in water - effects of minced muscle processing and test temperature. J Food Sci 59(4):777-80.
    • (1994) J Food Sci , vol.59 , Issue.4 , pp. 777-780
    • Howe, J.1    Hamann, D.2    Lanier, T.3    Park, J.4
  • 14
    • 78649478080 scopus 로고    scopus 로고
    • Effects of muscle fiber types on gel property of surimi-like materials from chicken, pork and beef
    • Kang G, Park G, Joo S, Lee M, Lee S. 2010. Effects of muscle fiber types on gel property of surimi-like materials from chicken, pork and beef. J Muscle Foods 21(3):570-84.
    • (2010) J Muscle Foods , vol.21 , Issue.3 , pp. 570-584
    • Kang, G.1    Park, G.2    Joo, S.3    Lee, M.4    Lee, S.5
  • 17
    • 84986456114 scopus 로고
    • Thermal gelation of pork, beef, fish, chicken and turkey muscles as affected by heating rate and pH
    • Lan YH, Novakofski J, Mccusker RH, Brewer MS, Carr TR, Mckeith FK. 1995b. Thermal gelation of pork, beef, fish, chicken and turkey muscles as affected by heating rate and pH. J Food Sci 60(5):936-40.
    • (1995) J Food Sci , vol.60 , Issue.5 , pp. 936-940
    • Lan, Y.H.1    Novakofski, J.2    Mccusker, R.H.3    Brewer, M.S.4    Carr, T.R.5    Mckeith, F.K.6
  • 18
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • In: Park JW, editor. 2nd ed. Boca Raton, FL: Taylor & Francis/CRC.
    • Lanier TC, Carvajal P, Yongsawatdigul J. 2005. Surimi gelation chemistry. In: Park JW, editor. Surimi and surimi seafood. 2nd ed. Boca Raton, FL: Taylor & Francis/CRC. p 435-89.
    • (2005) Surimi and surimi seafood , pp. 435-489
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 19
    • 0041985605 scopus 로고
    • Gelation of turkey breast and thigh myofibrils - effects of pH, salt and temperature
    • Lavelle CL, Foegeding EA. 1993. Gelation of turkey breast and thigh myofibrils - effects of pH, salt and temperature. J Food Sci 58(4):727-30.
    • (1993) J Food Sci , vol.58 , Issue.4 , pp. 727-730
    • Lavelle, C.L.1    Foegeding, E.A.2
  • 20
    • 79951772079 scopus 로고    scopus 로고
    • Comparative study on the stability of fish actomyosin and pork actomyosin
    • Liu R, Zhao S, Yang H, Li D, Xiong S, Xie B. 2011. Comparative study on the stability of fish actomyosin and pork actomyosin. Meat Sci 88(2):234-40.
    • (2011) Meat Sci , vol.88 , Issue.2 , pp. 234-240
    • Liu, R.1    Zhao, S.2    Yang, H.3    Li, D.4    Xiong, S.5    Xie, B.6
  • 21
    • 34548490104 scopus 로고    scopus 로고
    • Studies on fish and pork paste gelation by dynamic rheology and circular dichroism
    • Liu R, Zhao S, Xiong S, Xie B, Liu H. 2007. Studies on fish and pork paste gelation by dynamic rheology and circular dichroism. J Food Sci 72(7):E399-403.
    • (2007) J Food Sci , vol.72 , Issue.7
    • Liu, R.1    Zhao, S.2    Xiong, S.3    Xie, B.4    Liu, H.5
  • 22
    • 4744351115 scopus 로고    scopus 로고
    • Rapid heating effects on gelation of muscle proteins
    • Riemann AE, Lanier TC, Swartzel KR. 2004. Rapid heating effects on gelation of muscle proteins. J Food Sci 69(7):E308-14.
    • (2004) J Food Sci , vol.69 , Issue.7
    • Riemann, A.E.1    Lanier, T.C.2    Swartzel, K.R.3
  • 23
    • 84989992648 scopus 로고
    • Heat gelling properties of myosin, actin, actomyosin and myosin-subunits in a saline model system
    • Samejima K, Hashimot Y, Yasui T, Fukazawa T. 1969. Heat gelling properties of myosin, actin, actomyosin and myosin-subunits in a saline model system. J Food Sci 34(3):242-5.
    • (1969) J Food Sci , vol.34 , Issue.3 , pp. 242-245
    • Samejima, K.1    Hashimot, Y.2    Yasui, T.3    Fukazawa, T.4
  • 24
    • 84985265332 scopus 로고
    • Dynamic viscoelastic behavior of F-actin on heating
    • Sano T, Noguchi SF, Matsumoto JJ, Tsuchiya T. 1989. Dynamic viscoelastic behavior of F-actin on heating. J Food Sci 54(1):231-2.
    • (1989) J Food Sci , vol.54 , Issue.1 , pp. 231-232
    • Sano, T.1    Noguchi, S.F.2    Matsumoto, J.J.3    Tsuchiya, T.4
  • 25
    • 84987300642 scopus 로고
    • Thermal gelation characteristics of myosin subfragments
    • Sano T, Noguchi SF, Matsumoto JJ, Tsuchiya T. 1990. Thermal gelation characteristics of myosin subfragments. J Food Sci 55(1):55-8.
    • (1990) J Food Sci , vol.55 , Issue.1 , pp. 55-58
    • Sano, T.1    Noguchi, S.F.2    Matsumoto, J.J.3    Tsuchiya, T.4
  • 26
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano T, Noguchi SF, Tsuchiya T, Matsumoto JJ. 1988. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J Food Sci 53(3):924-8.
    • (1988) J Food Sci , vol.53 , Issue.3 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 27
    • 0000254629 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments
    • Smyth AB, Smith DM, VegaWarner V, ONeill E. 1996. Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments. J Agric Food Chem 44(4):1005-10.
    • (1996) J Agric Food Chem , vol.44 , Issue.4 , pp. 1005-1010
    • Smyth, A.B.1    Smith, D.M.2    VegaWarner, V.3    ONeill, E.4
  • 28
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollock myosin and light meromyosin
    • Togashi M, Kakinuma M, Nakaya M, Ooi T, Watabe S. 2002. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollock myosin and light meromyosin. J Agric Food Chem 50(17):4803-11.
    • (2002) J Agric Food Chem , vol.50 , Issue.17 , pp. 4803-4811
    • Togashi, M.1    Kakinuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 29
    • 0000741849 scopus 로고
    • Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heating
    • Wang SF, Smith DM. 1994. Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heating. J Agric Food Chem 42(7):1434-9.
    • (1994) J Agric Food Chem , vol.42 , Issue.7 , pp. 1434-1439
    • Wang, S.F.1    Smith, D.M.2
  • 30
    • 0003200724 scopus 로고
    • Myosin gelation kinetic-study based on rheological measurements
    • Wu JQ, Hamann DD, Foegeding EA. 1991. Myosin gelation kinetic-study based on rheological measurements. J Agric Food Chem 39(2):229-36.
    • (1991) J Agric Food Chem , vol.39 , Issue.2 , pp. 229-236
    • Wu, J.Q.1    Hamann, D.D.2    Foegeding, E.A.3
  • 31
    • 0001334692 scopus 로고
    • Dynamic gelling properties of myofibrillar protein from skeletal muscles of different chicken parts
    • Xiong YL, Blanchard SP. 1994a. Dynamic gelling properties of myofibrillar protein from skeletal muscles of different chicken parts. J Agric Food Chem 42(3):670-4.
    • (1994) J Agric Food Chem , vol.42 , Issue.3 , pp. 670-674
    • Xiong, Y.L.1    Blanchard, S.P.2
  • 32
    • 84985258656 scopus 로고
    • Myofibrillar protein gelation - viscoelastic changes related to heating procedures
    • Xiong YL, Blanchard SP. 1994b. Myofibrillar protein gelation - viscoelastic changes related to heating procedures. J Food Sci 59(4):734-8.
    • (1994) J Food Sci , vol.59 , Issue.4 , pp. 734-738
    • Xiong, Y.L.1    Blanchard, S.P.2
  • 33
    • 84985219440 scopus 로고
    • Protein extractability and thermally induced gelation properties of myofibrils isolated from prerigor and postrigor chicken muscles
    • Xiong YL, Brekke CJ. 1991. Protein extractability and thermally induced gelation properties of myofibrils isolated from prerigor and postrigor chicken muscles. J Food Sci 56(1):210-5.
    • (1991) J Food Sci , vol.56 , Issue.1 , pp. 210-215
    • Xiong, Y.L.1    Brekke, C.J.2
  • 34
    • 84986435961 scopus 로고
    • Heat-induced gelation of myosin in the presence of actin
    • Yasui T, Ishioroshi M, Samejima K. 1980. Heat-induced gelation of myosin in the presence of actin. J Food Biochem 4(2):61-78.
    • (1980) J Food Biochem , vol.4 , Issue.2 , pp. 61-78
    • Yasui, T.1    Ishioroshi, M.2    Samejima, K.3
  • 35
    • 0032867089 scopus 로고    scopus 로고
    • Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate
    • Yongsawatdigul J, Park JW. 1999. Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate. J Food Sci 64(4):679-683.
    • (1999) J Food Sci , vol.64 , Issue.4 , pp. 679-683
    • Yongsawatdigul, J.1    Park, J.W.2
  • 36
    • 4744349306 scopus 로고    scopus 로고
    • Water holding capacity of proteins
    • In: Zayas JF, editor. Berlin, Germany: Springer-Verlag Berlin Heidelberg.
    • Zayas JF. 1997. Water holding capacity of proteins. In: Zayas JF, editor. Functionality of proteins in food. Berlin, Germany: Springer-Verlag Berlin Heidelberg. p 76-133.
    • (1997) Functionality of proteins in food , pp. 76-133
    • Zayas, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.