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Volumn 188, Issue , 2015, Pages 111-118

Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure

Author keywords

Electrostatic interactions; High pressure; Hydrogen bond; Low field NMR; Myofibrillar protein; Water holding capacity

Indexed keywords

CHEMICAL BONDS; COULOMB INTERACTIONS; COVALENT BONDS; ELECTROSTATICS; HYDROGEN BONDS; HYDROPHOBICITY; PROTEINS;

EID: 84929459658     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.04.129     Document Type: Article
Times cited : (302)

References (37)
  • 1
    • 43149085977 scopus 로고    scopus 로고
    • High pressure gelation of soy proteins: Effect of concentration, pH and additives
    • P.A. Alvarez, H.S. Ramaswamy, and A.A. Ismail High pressure gelation of soy proteins: Effect of concentration, pH and additives Journal of Food Engineering 88 2008 331 340
    • (2008) Journal of Food Engineering , vol.88 , pp. 331-340
    • Alvarez, P.A.1    Ramaswamy, H.S.2    Ismail, A.A.3
  • 4
    • 0015522259 scopus 로고
    • Pulsed NMR studies of water in striated muscle. I. Transverse nuclear spin relaxation times and freezing effects
    • P.S. Belton, R.R. Jackson, and K.J. Packer Pulsed NMR studies of water in striated muscle. I. Transverse nuclear spin relaxation times and freezing effects Biochimica et Biophysica Acta 286 1 1972 16 25
    • (1972) Biochimica et Biophysica Acta , vol.286 , Issue.1 , pp. 16-25
    • Belton, P.S.1    Jackson, R.R.2    Packer, K.J.3
  • 8
    • 84987297811 scopus 로고
    • Cross-linking of myosin heavy chains from cod, herring and silver hake during thermal setting
    • J.K. Chan, T.A. Gill, and A.T. Paulson Cross-linking of myosin heavy chains from cod, herring and silver hake during thermal setting Journal of Food Science 57 4 1992 906 912
    • (1992) Journal of Food Science , vol.57 , Issue.4 , pp. 906-912
    • Chan, J.K.1    Gill, T.A.2    Paulson, A.T.3
  • 9
    • 0000872633 scopus 로고
    • Effects of high hydrostatic pressure on food constituents: An overview
    • C. Balny, R. Hayashi, K. Heremans, P. Masson, Colloque INSERM/John Libbey Eurotext Ltd
    • J.C. Cheftel Effects of high hydrostatic pressure on food constituents: An overview C. Balny, R. Hayashi, K. Heremans, P. Masson, High pressure and biotechnology 1992 Colloque INSERM/John Libbey Eurotext Ltd 195 209
    • (1992) High Pressure and Biotechnology , pp. 195-209
    • Cheftel, J.C.1
  • 10
    • 0031190812 scopus 로고    scopus 로고
    • Effects of high pressure on meat: A review
    • J.C. Cheftel, and J. Culioli Effects of high pressure on meat: A review Meat Science 46 3 1997 211 236
    • (1997) Meat Science , vol.46 , Issue.3 , pp. 211-236
    • Cheftel, J.C.1    Culioli, J.2
  • 11
    • 3042652596 scopus 로고
    • Variations of SH content and kamaboko-gel forming ability of shark muscle proteins by electrolysis
    • M. Hamada, S. Ishizaki, and T. Nagai Variations of SH content and kamaboko-gel forming ability of shark muscle proteins by electrolysis The Journal of Shimonoseki University of Fisheries 42 3 1994 131 135
    • (1994) The Journal of Shimonoseki University of Fisheries , vol.42 , Issue.3 , pp. 131-135
    • Hamada, M.1    Ishizaki, S.2    Nagai, T.3
  • 12
  • 13
    • 84904661583 scopus 로고    scopus 로고
    • Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics
    • M.Y. Han, P. Wang, X.L. Xu, and G.H. Zhou Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics Food Research International 62 2014 1175 1182
    • (2014) Food Research International , vol.62 , pp. 1175-1182
    • Han, M.Y.1    Wang, P.2    Xu, X.L.3    Zhou, G.H.4
  • 14
    • 39149135215 scopus 로고    scopus 로고
    • Raman spectroscopy study of the structural effect of microbial transglutaminase on meat systems and its relationship with textural characteristics
    • A.M. Herrero, M.I. Cambero, J.A. Ordonez, L. de la Hoz, and P. Carmona Raman spectroscopy study of the structural effect of microbial transglutaminase on meat systems and its relationship with textural characteristics Food Chemistry 109 1 2008 25 32
    • (2008) Food Chemistry , vol.109 , Issue.1 , pp. 25-32
    • Herrero, A.M.1    Cambero, M.I.2    Ordonez, J.A.3    De La Hoz, L.4    Carmona, P.5
  • 15
    • 84885724866 scopus 로고    scopus 로고
    • Effects of high pressure on the physicochemical and functional properties of peanut protein isolates
    • X.H. He, H.Z. Liu, L. Liu, G.L. Zhao, Q. Wang, and Q.L. Chen Effects of high pressure on the physicochemical and functional properties of peanut protein isolates Food Hydrocolloids 36 2014 123 129
    • (2014) Food Hydrocolloids , vol.36 , pp. 123-129
    • He, X.H.1    Liu, H.Z.2    Liu, L.3    Zhao, G.L.4    Wang, Q.5    Chen, Q.L.6
  • 16
    • 33846967090 scopus 로고    scopus 로고
    • Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Oreochromis niloticus) on hydrostatic pressure treatment
    • K.C. Hsu, J.S. Hwang, C.C. Yu, and C.L. Jao Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Oreochromis niloticus) on hydrostatic pressure treatment Food Chemistry 103 2007 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
  • 17
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels
    • S. Ikeda, and E.C.Y. Li-Chan Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels Food Hydrocolloids 18 3 2004 489 498
    • (2004) Food Hydrocolloids , vol.18 , Issue.3 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.Y.2
  • 18
    • 0001064628 scopus 로고
    • Microcentrifuge-based method for measuring water-holding of protein gels
    • P.N. Kocher, and E.A. Foegeding Microcentrifuge-based method for measuring water-holding of protein gels Journal of Food Science 58 5 1993 1040 1046
    • (1993) Journal of Food Science , vol.58 , Issue.5 , pp. 1040-1046
    • Kocher, P.N.1    Foegeding, E.A.2
  • 19
    • 0038528591 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on molecular conformation of tilapia (Oreochromis niloticus) myosin
    • W.C. Ko, C.L. Jao, and K.C. Hsu Effect of hydrostatic pressure on molecular conformation of tilapia (Oreochromis niloticus) myosin Journal of Food Science 68 4 2003 1192 1195
    • (2003) Journal of Food Science , vol.68 , Issue.4 , pp. 1192-1195
    • Ko, W.C.1    Jao, C.L.2    Hsu, K.C.3
  • 20
    • 34248394702 scopus 로고    scopus 로고
    • Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment
    • W.C. Ko, C.C. Yu, and K.C. Hsu Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment LWT-Food Science and Technology 40 2007 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
  • 21
    • 33846080109 scopus 로고    scopus 로고
    • Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment
    • J. Lee, Y.J. Kim, N.H. Lee, S.I. Hong, and K. Yamamoto Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment Journal of the Science of Food and Agriculture 87 2007 40 46
    • (2007) Journal of the Science of Food and Agriculture , vol.87 , pp. 40-46
    • Lee, J.1    Kim, Y.J.2    Lee, N.H.3    Hong, S.I.4    Yamamoto, K.5
  • 22
    • 0030295334 scopus 로고    scopus 로고
    • The applications of Raman spectroscopy in food science
    • E.C.Y. Li-Chan The applications of Raman spectroscopy in food science Trends in Food Science and Technology 7 11 1996 361 370
    • (1996) Trends in Food Science and Technology , vol.7 , Issue.11 , pp. 361-370
    • Li-Chan, E.C.Y.1
  • 24
    • 79952536911 scopus 로고    scopus 로고
    • Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties
    • R. Liu, S.M. Zhao, B.J. Xie, and S.B. Xiong Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties Food Hydrocolloids 25 2011 898 906
    • (2011) Food Hydrocolloids , vol.25 , pp. 898-906
    • Liu, R.1    Zhao, S.M.2    Xie, B.J.3    Xiong, S.B.4
  • 25
    • 0000556763 scopus 로고
    • Binding of comminuted meat: Effect of high pressure
    • J.J. Macfarlane, I.J. Mckenzie, and R.H. Turner Binding of comminuted meat: Effect of high pressure Meat Science 10 1984 307 320
    • (1984) Meat Science , vol.10 , pp. 307-320
    • Macfarlane, J.J.1    McKenzie, I.J.2    Turner, R.H.3
  • 26
    • 77049107297 scopus 로고    scopus 로고
    • High pressure induced changes on sarcoplasmic protein fraction and quality indicators
    • B. Marcos, J.P. Kerry, and A.M. Mullen High pressure induced changes on sarcoplasmic protein fraction and quality indicators Meat Science 85 2010 115 120
    • (2010) Meat Science , vol.85 , pp. 115-120
    • Marcos, B.1    Kerry, J.P.2    Mullen, A.M.3
  • 27
    • 0019484519 scopus 로고
    • The theory of pressure effects on enzymes
    • E. Morild The theory of pressure effects on enzymes Advances in Protein Chemistry 34 1981 93 166
    • (1981) Advances in Protein Chemistry , vol.34 , pp. 93-166
    • Morild, E.1
  • 32
    • 77954383543 scopus 로고    scopus 로고
    • Theoretical aspects of water-holding in meat
    • E. Puolanne, and M. Halonen Theoretical aspects of water-holding in meat Meat Science 86 2010 151 165
    • (2010) Meat Science , vol.86 , pp. 151-165
    • Puolanne, E.1    Halonen, M.2
  • 34
    • 85007905278 scopus 로고
    • Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye Pollack surimi paste
    • J. Wan, I. Kimura, and M. Satake Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye Pollack surimi paste Fisheries Science 60 1994 107 112
    • (1994) Fisheries Science , vol.60 , pp. 107-112
    • Wan, J.1    Kimura, I.2    Satake, M.3
  • 35
    • 0034064983 scopus 로고    scopus 로고
    • Protein extraction from chicken myofibrils irrigated with various poly phosphate and NaCl solutions
    • Y.L. Xiong, X. Lou, and C. Wang Protein extraction from chicken myofibrils irrigated with various poly phosphate and NaCl solutions Food Chemistry and Toxicology 65 1 2000 96 100
    • (2000) Food Chemistry and Toxicology , vol.65 , Issue.1 , pp. 96-100
    • Xiong, Y.L.1    Lou, X.2    Wang, C.3
  • 36
    • 84985200251 scopus 로고
    • Changes in shear modulus, ultrastructure and spin-spin relaxation times of water associated with heat-induced gelation of myosin
    • T. Yasui, M. Ishioroshi, H. Nakano, and K. Samejima Changes in shear modulus, ultrastructure and spin-spin relaxation times of water associated with heat-induced gelation of myosin Journal of Food Science 44 4 1979 1201 1204
    • (1979) Journal of Food Science , vol.44 , Issue.4 , pp. 1201-1204
    • Yasui, T.1    Ishioroshi, M.2    Nakano, H.3    Samejima, K.4
  • 37
    • 84896855099 scopus 로고    scopus 로고
    • Physicochemical properties of natural actomyosin from threadfin bream (Nemipterus spp.) induced by high hydrostatic pressure
    • A.M. Zhou, L.Y. Lin, Y. Liang, S. Benjakul, X.L. Shi, and X. Liu Physicochemical properties of natural actomyosin from threadfin bream (Nemipterus spp.) induced by high hydrostatic pressure Food Chemistry 156 2014 402 407
    • (2014) Food Chemistry , vol.156 , pp. 402-407
    • Zhou, A.M.1    Lin, L.Y.2    Liang, Y.3    Benjakul, S.4    Shi, X.L.5    Liu, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.