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Volumn 134, Issue 2, 2012, Pages 1005-1010

Aggregation and structural changes of silver carp actomyosin as affected by mild acidification with d-gluconic acid δ-lactone

Author keywords

Acidification; Actomyosin; Aggregation; Silver carp; Structural changes

Indexed keywords

ACIDIC CONDITIONS; ACTOMYOSIN; AGGREGATION PROPERTY; CARBODIIMIDES; D-GLUCONIC ACIDS; ELECTROPHORESIS ANALYSIS; HELICAL CONTENT; INTRINSIC FLUORESCENCE; MYOSIN HEAVY CHAIN; POLAR ENVIRONMENTS; PROTEIN AGGREGATES; PROTEIN COMPONENTS; SILVER CARP; STRUCTURAL CHANGE; TERTIARY STRUCTURES; TRYPTOPHAN RESIDUES; TYROSINE RESIDUES; UV SPECTRUM;

EID: 84862811886     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.02.216     Document Type: Article
Times cited : (70)

References (42)
  • 3
    • 0000592111 scopus 로고    scopus 로고
    • Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acidic conditions
    • S.P. Chawla, V. Venugopal, and P.M. Nair Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acidic conditions Journal of Food Science 61 2 1996 362 367
    • (1996) Journal of Food Science , vol.61 , Issue.2 , pp. 362-367
    • Chawla, S.P.1    Venugopal, V.2    Nair, P.M.3
  • 4
    • 0024786754 scopus 로고
    • Thermal aggregation of cod (Gadus morhud) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker
    • T.A. Gill, and J.T. Conway Thermal aggregation of cod (Gadus morhud) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker Agricultural and Biological Chemistry 53 10 1989 2553 2562
    • (1989) Agricultural and Biological Chemistry , vol.53 , Issue.10 , pp. 2553-2562
    • Gill, T.A.1    Conway, J.T.2
  • 6
    • 0042061104 scopus 로고    scopus 로고
    • Effect of low and high pH treatment on the functional properties of cod muscle proteins
    • H.G. Kristinsson, and H.O. Hultin Effect of low and high pH treatment on the functional properties of cod muscle proteins Journal of Agricultural and Food Chemistry 51 2003 5103 5110
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 5103-5110
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 5259 1970 680 685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 34250748371 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles
    • F. Lefevre, B. Fauconneau, J.W. Thompson, and T.A. Gill Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles Journal of Agricultural and Food Chemistry 55 12 2007 4761 4770
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.12 , pp. 4761-4770
    • Lefevre, F.1    Fauconneau, B.2    Thompson, J.W.3    Gill, T.A.4
  • 9
    • 0001475995 scopus 로고    scopus 로고
    • Lipid oxidation and myosin denaturation in dark chicken meat
    • S.J. Li, and A.J. King Lipid oxidation and myosin denaturation in dark chicken meat Journal of Agricultural and Food Chemistry 44 10 1996 3080 3084
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.10 , pp. 3080-3084
    • Li, S.J.1    King, A.J.2
  • 10
    • 75749097238 scopus 로고    scopus 로고
    • Effect of pH on the gel properties and secondary structure of fish myosin
    • R. Liu, S.M. Zhao, Y.M. Liu, H. Yang, S.B. Xiong, and B.J. Xie Effect of pH on the gel properties and secondary structure of fish myosin Food Chemistry 121 1 2010 196 202
    • (2010) Food Chemistry , vol.121 , Issue.1 , pp. 196-202
    • Liu, R.1    Zhao, S.M.2    Liu, Y.M.3    Yang, H.4    Xiong, S.B.5    Xie, B.J.6
  • 11
    • 50249126674 scopus 로고    scopus 로고
    • Role of secondary structures in the gelation of porcine myosin at different pH values
    • R. Liu, S.M. Zhao, S.B. Xiong, B.J. Xie, and L.H. Qin Role of secondary structures in the gelation of porcine myosin at different pH values Meat Science 80 3 2008 632 639
    • (2008) Meat Science , vol.80 , Issue.3 , pp. 632-639
    • Liu, R.1    Zhao, S.M.2    Xiong, S.B.3    Xie, B.J.4    Qin, L.H.5
  • 12
    • 79951772079 scopus 로고    scopus 로고
    • Comparative study on the stability of fish actomyosin and pork actomyosin
    • R. Liu, S.M. Zhao, H. Yang, D.D. Li, S.B. Xiong, and B.J. Xie Comparative study on the stability of fish actomyosin and pork actomyosin Meat Science 88 2 2011 234 240
    • (2011) Meat Science , vol.88 , Issue.2 , pp. 234-240
    • Liu, R.1    Zhao, S.M.2    Yang, H.3    Li, D.D.4    Xiong, S.B.5    Xie, B.J.6
  • 13
    • 0027996853 scopus 로고
    • Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy
    • H. Mach, and C.R. Middaugh Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy Analytical Biochemistry 222 2 1994 323 331
    • (1994) Analytical Biochemistry , vol.222 , Issue.2 , pp. 323-331
    • MacH, H.1    Middaugh, C.R.2
  • 14
    • 34347247653 scopus 로고    scopus 로고
    • Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)
    • M. Mohan, D. Ramachandran, T.V. Sankar, and R. Anandan Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus) Process Biochemistry 42 2007 1056 1062
    • (2007) Process Biochemistry , vol.42 , pp. 1056-1062
    • Mohan, M.1    Ramachandran, D.2    Sankar, T.V.3    Anandan, R.4
  • 15
    • 0030507501 scopus 로고    scopus 로고
    • 1,5-Glucono-δ-lactone-induced gelation of myofibrillar protein at chilled temperatures
    • T.M. Ngapo, B.H.P. Wilkinson, and R. Chong 1,5-Glucono-δ-lactone- induced gelation of myofibrillar protein at chilled temperatures Meat Science 42 1 1996 3 13
    • (1996) Meat Science , vol.42 , Issue.1 , pp. 3-13
    • Ngapo, T.M.1    Wilkinson, B.H.P.2    Chong, R.3
  • 18
    • 0002083553 scopus 로고    scopus 로고
    • Rheological and biochemical characteristics of high-pressure- and heat-induced gels from blue whiting (Micromesistius poutassou) muscle proteins
    • M. Pérez-Mateos, H. Loureno, P. Montero, and A.J. Borderias Rheological and biochemical characteristics of high-pressure- and heat-induced gels from blue whiting (Micromesistius poutassou) muscle proteins Journal of Agricultural and Food Chemistry 45 1 1997 44 49
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.1 , pp. 44-49
    • Pérez-Mateos, M.1    Loureno, H.2    Montero, P.3    Borderias, A.J.4
  • 19
    • 34249865663 scopus 로고    scopus 로고
    • Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding
    • S. Raghavan, and H.G. Kristinsson Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding Journal of Agricultural and Food Chemistry 55 10 2007 4144 4153
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.10 , pp. 4144-4153
    • Raghavan, S.1    Kristinsson, H.G.2
  • 20
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second derivative spectroscopy
    • R. Ragone, G. Colonna, C. Balestrier, L. Servillo, and G. Irace Determination of tyrosine exposure in proteins by second derivative spectroscopy Biochemistry 23 1984 1871 1875
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrier, C.3    Servillo, L.4    Irace, G.5
  • 23
    • 38049160213 scopus 로고    scopus 로고
    • Properties and acceptability of Som-fug, a Thai fermented fish mince, inoculated with lactic acid bacteria starters
    • S. Riebroy, S. Benjakula, and W. Visessanguan Properties and acceptability of Som-fug, a Thai fermented fish mince, inoculated with lactic acid bacteria starters LWT-Food Science and Technology 41 4 2008 569 580
    • (2008) LWT-Food Science and Technology , vol.41 , Issue.4 , pp. 569-580
    • Riebroy, S.1    Benjakula, S.2    Visessanguan, W.3
  • 24
    • 39149097500 scopus 로고    scopus 로고
    • Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota)
    • S. Riebroy, S. Benjakula, W. Visessanguanb, U. Eriksonc, and T. Rustad Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota) Food Chemistry 109 1 2008 42 53
    • (2008) Food Chemistry , vol.109 , Issue.1 , pp. 42-53
    • Riebroy, S.1    Benjakula, S.2    Visessanguanb, W.3    Eriksonc, U.4    Rustad, T.5
  • 25
    • 48049085689 scopus 로고    scopus 로고
    • Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota)
    • S. Riebroy, S. Benjakula, W. Visessanguanb, U. Eriksonc, and T. Rustad Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota) Food Hydrocolloids 23 1 2009 26 39
    • (2009) Food Hydrocolloids , vol.23 , Issue.1 , pp. 26-39
    • Riebroy, S.1    Benjakula, S.2    Visessanguanb, W.3    Eriksonc, U.4    Rustad, T.5
  • 26
    • 33745037483 scopus 로고    scopus 로고
    • Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack
    • Y. Satoh, M. Nakaya, Y. Ochiai, and S. Watabe Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack Fisheries Science 72 3 2006 646 655
    • (2006) Fisheries Science , vol.72 , Issue.3 , pp. 646-655
    • Satoh, Y.1    Nakaya, M.2    Ochiai, Y.3    Watabe, S.4
  • 27
    • 38149143277 scopus 로고
    • The effect of acidification on myofibrillar proteins
    • A.B. Saunders The effect of acidification on myofibrillar proteins Meat Science 37 1994 271 280
    • (1994) Meat Science , vol.37 , pp. 271-280
    • Saunders, A.B.1
  • 28
    • 79955635922 scopus 로고    scopus 로고
    • Effect of setting conditions on mechanical properties of acid-induced Kamaboko gel from squid Todarodes pacificus mantle muscle meat
    • B. Techaratanakrai, M. Nishida, Y. Igarashi, M. Watanabe, E. Okazaki, and K. Osako Effect of setting conditions on mechanical properties of acid-induced Kamaboko gel from squid Todarodes pacificus mantle muscle meat Fisheries Science 77 3 2011 439 446
    • (2011) Fisheries Science , vol.77 , Issue.3 , pp. 439-446
    • Techaratanakrai, B.1    Nishida, M.2    Igarashi, Y.3    Watanabe, M.4    Okazaki, E.5    Osako, K.6
  • 29
    • 53149105485 scopus 로고    scopus 로고
    • Effect of inulin on the rheological properties of silken tofu coagulated with glucono-d-lactone
    • Y.C. Tseng, and Y.L. Xiong Effect of inulin on the rheological properties of silken tofu coagulated with glucono-d-lactone Journal of Food Engineering 90 2009 511 516
    • (2009) Journal of Food Engineering , vol.90 , pp. 511-516
    • Tseng, Y.C.1    Xiong, Y.L.2
  • 30
    • 0037172348 scopus 로고    scopus 로고
    • An overview of small-scale food fermentation technologies in developing countries with special reference to Thailand: Scope for their improvement
    • R. Valyasevi, and R.S. Rolle An overview of small-scale food fermentation technologies in developing countries with special reference to Thailand: Scope for their improvement International Journal of Food Microbiology 75 3 2002 231 239
    • (2002) International Journal of Food Microbiology , vol.75 , Issue.3 , pp. 231-239
    • Valyasevi, R.1    Rolle, R.S.2
  • 31
    • 0028265237 scopus 로고
    • Gelation of shark myofibrillar proteins by weak organic acids
    • V. Venugopal, S.N. Doke, and P.M. Nair Gelation of shark myofibrillar proteins by weak organic acids Food Chemistry 50 2 1994 185 190
    • (1994) Food Chemistry , vol.50 , Issue.2 , pp. 185-190
    • Venugopal, V.1    Doke, S.N.2    Nair, P.M.3
  • 32
  • 33
    • 11144317965 scopus 로고    scopus 로고
    • Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin
    • V. Vetri, and V. Militello Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin Biophysical Chemistry 113 1 2005 83 91
    • (2005) Biophysical Chemistry , vol.113 , Issue.1 , pp. 83-91
    • Vetri, V.1    Militello, V.2
  • 34
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin
    • W. Visessanguan, M. Ogawa, S. Nakai, and H. An Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin Journal of Agricultural and Food Chemistry 48 4 2000 1016 1023
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.4 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4
  • 35
    • 79959253717 scopus 로고    scopus 로고
    • Effect of glucono-delta-lactone acidification and heat treatment on the physicochemical properties of silver carp mince
    • Y.S. Xu, Q.X. Jiang, and W.S. Xia Effect of glucono-delta-lactone acidification and heat treatment on the physicochemical properties of silver carp mince LWT-Food Science and Technology 44 9 2011 1952 1957
    • (2011) LWT-Food Science and Technology , vol.44 , Issue.9 , pp. 1952-1957
    • Xu, Y.S.1    Jiang, Q.X.2    Xia, W.S.3
  • 36
    • 80355125305 scopus 로고    scopus 로고
    • Acid-induced aggregation of actomyosin from silver carp (Hypophthalmichthys molitrix)
    • Y.S. Xu, W.S. Xia, Q.X. Jiang, and S.Q. Rao Acid-induced aggregation of actomyosin from silver carp (Hypophthalmichthys molitrix) Food Hydrocolloids 27 2 2012 309 315
    • (2012) Food Hydrocolloids , vol.27 , Issue.2 , pp. 309-315
    • Xu, Y.S.1    Xia, W.S.2    Jiang, Q.X.3    Rao, S.Q.4
  • 37
    • 69349104713 scopus 로고    scopus 로고
    • Effect of fermentation temperature on the microbial and physicochemical properties of silver carp sausages inoculated with Pediococcus pentosaceus
    • Y.S. Xu, W.S. Xia, F. Yang, J.M. Kim, and X.H. Nie Effect of fermentation temperature on the microbial and physicochemical properties of silver carp sausages inoculated with Pediococcus pentosaceus Food Chemistry 118 3 2010 512 518
    • (2010) Food Chemistry , vol.118 , Issue.3 , pp. 512-518
    • Xu, Y.S.1    Xia, W.S.2    Yang, F.3    Kim, J.M.4    Nie, X.H.5
  • 38
    • 74149083792 scopus 로고    scopus 로고
    • Protein molecular interactions involved in the gel network formation of fermented silver carp mince inoculated with Pediococcus pentosaceus
    • Y.S. Xu, W.S. Xia, F. Yang, and X.H. Nie Protein molecular interactions involved in the gel network formation of fermented silver carp mince inoculated with Pediococcus pentosaceus Food Chemistry 120 3 2010 717 723
    • (2010) Food Chemistry , vol.120 , Issue.3 , pp. 717-723
    • Xu, Y.S.1    Xia, W.S.2    Yang, F.3    Nie, X.H.4
  • 39
    • 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
    • S. Yarnpakdee, S. Benjakul, W. Visessanguan, and K. Kijroongrojana Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish (Mulloidichthys martinicus) muscle as influenced by iced storage Food Hydrocolloids 23 7 2009 1779 1784
    • (2009) Food Hydrocolloids , vol.23 , Issue.7 , pp. 1779-1784
    • Yarnpakdee, S.1    Benjakul, S.2    Visessanguan, W.3    Kijroongrojana, K.4
  • 40
    • 0036216284 scopus 로고    scopus 로고
    • Effect of lactic acid bacterial fermentation on the characteristics of minced mackerel
    • L.J. Yin, C.L. Pan, and S.T. Jiang Effect of lactic acid bacterial fermentation on the characteristics of minced mackerel Journal of Food Science 67 2 2002 786 792
    • (2002) Journal of Food Science , vol.67 , Issue.2 , pp. 786-792
    • Yin, L.J.1    Pan, C.L.2    Jiang, S.T.3
  • 41
    • 0041386023 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of threadfin bream actomyosin
    • J. Yongsawatdigul, and J.W. Park Thermal denaturation and aggregation of threadfin bream actomyosin Food Chemistry 83 3 2003 409 416
    • (2003) Food Chemistry , vol.83 , Issue.3 , pp. 409-416
    • Yongsawatdigul, J.1    Park, J.W.2
  • 42
    • 41949138699 scopus 로고    scopus 로고
    • The effect of pulsed electric fields on the inactivation and structure of lysozyme
    • W. Zhao, and R.J. Yang The effect of pulsed electric fields on the inactivation and structure of lysozyme Food Chemistry 110 2 2008 334 343
    • (2008) Food Chemistry , vol.110 , Issue.2 , pp. 334-343
    • Zhao, W.1    Yang, R.J.2


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