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Volumn 83, Issue , 2016, Pages 152-161

Effects of konjac glucomannan on heat-induced changes of physicochemical and structural properties of surimi gels

Author keywords

Deacetylated; High temperature; Konjac glucomannan; Physicochemical and structural properties; Surimi gels

Indexed keywords

COVALENT BONDS; GELS; HYDROGEN BONDS; HYDROPHOBICITY; LASER OPTICS; STRUCTURAL PROPERTIES; X RAY DIFFRACTION;

EID: 84960471079     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2016.03.007     Document Type: Article
Times cited : (156)

References (69)
  • 1
    • 0001021914 scopus 로고
    • Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band
    • Alix A.J.P., Pedanou G., Berjot M. Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band. Journal of Molecular Structure 1988, 174:159-164.
    • (1988) Journal of Molecular Structure , vol.174 , pp. 159-164
    • Alix, A.J.P.1    Pedanou, G.2    Berjot, M.3
  • 3
    • 32944474540 scopus 로고    scopus 로고
    • Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins
    • Badii F., Howell N.K. Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids 2006, 20(5):630-640.
    • (2006) Food Hydrocolloids , vol.20 , Issue.5 , pp. 630-640
    • Badii, F.1    Howell, N.K.2
  • 6
    • 84876325390 scopus 로고    scopus 로고
    • Effect of different protein extracts from Dosidicus gigas muscle co-products on edible films development
    • Blanco-Pascual N., Fernández-Martín F., Montero M.P. Effect of different protein extracts from Dosidicus gigas muscle co-products on edible films development. Food Hydrocolloids 2013, 33(1):118-131.
    • (2013) Food Hydrocolloids , vol.33 , Issue.1 , pp. 118-131
    • Blanco-Pascual, N.1    Fernández-Martín, F.2    Montero, M.P.3
  • 7
    • 0030829061 scopus 로고    scopus 로고
    • In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy
    • Bouraoui M., Nakai S., Li-Chan E. In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy. Food Research International 1997, 30(1):65-72.
    • (1997) Food Research International , vol.30 , Issue.1 , pp. 65-72
    • Bouraoui, M.1    Nakai, S.2    Li-Chan, E.3
  • 9
    • 79955011039 scopus 로고    scopus 로고
    • Combining protein micro-phase separation and protein-polysaccharide segregative phase separation to produce gel structures
    • Çakir E., Foegeding E.A. Combining protein micro-phase separation and protein-polysaccharide segregative phase separation to produce gel structures. Food Hydrocolloids 2011, 25(6):1538-1546.
    • (2011) Food Hydrocolloids , vol.25 , Issue.6 , pp. 1538-1546
    • Çakir, E.1    Foegeding, E.A.2
  • 10
    • 0031630398 scopus 로고    scopus 로고
    • X-ray diffraction of food polysaccharides
    • Academic Press, L.T. Steve (Ed.)
    • Chandrasekaran R. X-ray diffraction of food polysaccharides. Advances in food and nutrition research 1998, Vol. 42:131-210. Academic Press. L.T. Steve (Ed.).
    • (1998) Advances in food and nutrition research , vol.42 , pp. 131-210
    • Chandrasekaran, R.1
  • 11
    • 79960564631 scopus 로고    scopus 로고
    • Identification of molecular driving forces involved in the gelation of konjac glucomannan: effect of degree of deacetylation on hydrophobic association
    • Chen J., Li J., Li B. Identification of molecular driving forces involved in the gelation of konjac glucomannan: effect of degree of deacetylation on hydrophobic association. Carbohydrate Polymers 2011, 86(2):865-871.
    • (2011) Carbohydrate Polymers , vol.86 , Issue.2 , pp. 865-871
    • Chen, J.1    Li, J.2    Li, B.3
  • 12
    • 57049132607 scopus 로고    scopus 로고
    • Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation
    • Chin K.B., Go M.Y., Xiong Y.L. Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation. Meat Science 2009, 81(3):565-572.
    • (2009) Meat Science , vol.81 , Issue.3 , pp. 565-572
    • Chin, K.B.1    Go, M.Y.2    Xiong, Y.L.3
  • 13
    • 0033831501 scopus 로고    scopus 로고
    • Evaluation of konjac blends and soy protein isolate as fat replacements in low-fat Bologna
    • Chin K.B., Keeton J.T., Miller R.K., Longnecker M.T., Lamkey J.W. Evaluation of konjac blends and soy protein isolate as fat replacements in low-fat Bologna. Journal of Food Science 2000, 65(5):756-763.
    • (2000) Journal of Food Science , vol.65 , Issue.5 , pp. 756-763
    • Chin, K.B.1    Keeton, J.T.2    Miller, R.K.3    Longnecker, M.T.4    Lamkey, J.W.5
  • 14
    • 0032031224 scopus 로고    scopus 로고
    • Liquid crystalline, rheological and thermal properties of konjac glucomannan
    • Dave V., Sheth M., McCarthy S.P., Ratto J.A., Kaplan D.L. Liquid crystalline, rheological and thermal properties of konjac glucomannan. Polymer 1998, 39(5):1139-1148.
    • (1998) Polymer , vol.39 , Issue.5 , pp. 1139-1148
    • Dave, V.1    Sheth, M.2    McCarthy, S.P.3    Ratto, J.A.4    Kaplan, D.L.5
  • 16
    • 84862799405 scopus 로고    scopus 로고
    • Effect of degree of deacetylation on physicochemical and gelation properties of konjac glucomannan
    • Du X., Li J., Chen J., Li B. Effect of degree of deacetylation on physicochemical and gelation properties of konjac glucomannan. Food Research International 2012, 46(1):270-278.
    • (2012) Food Research International , vol.46 , Issue.1 , pp. 270-278
    • Du, X.1    Li, J.2    Chen, J.3    Li, B.4
  • 17
    • 84898774871 scopus 로고    scopus 로고
    • Shrimp (Litopenaeus vannamei) muscle proteins as source to develop edible films
    • Gómez-Estaca J., Montero P., Gómez-Guillén M.C. Shrimp (Litopenaeus vannamei) muscle proteins as source to develop edible films. Food Hydrocolloids 2014, 41:86-94.
    • (2014) Food Hydrocolloids , vol.41 , pp. 86-94
    • Gómez-Estaca, J.1    Montero, P.2    Gómez-Guillén, M.C.3
  • 18
    • 0038277656 scopus 로고    scopus 로고
    • Thermal gelation properties of two different composition sardine (Sardina pilchardus) muscles with addition of non-muscle proteins and hydrocolloids
    • Gómez-Guillén C., Borderías A.J., Montera P. Thermal gelation properties of two different composition sardine (Sardina pilchardus) muscles with addition of non-muscle proteins and hydrocolloids. Food Chemistry 1997, 58(1):81-87.
    • (1997) Food Chemistry , vol.58 , Issue.1 , pp. 81-87
    • Gómez-Guillén, C.1    Borderías, A.J.2    Montera, P.3
  • 19
    • 0031231846 scopus 로고    scopus 로고
    • Chemical interactions of nonmuscle proteins in the network of sardine (Sardina pilchardus) muscle gels
    • Gómez-Guillén M.C., Borderías A.J., Montero P. Chemical interactions of nonmuscle proteins in the network of sardine (Sardina pilchardus) muscle gels. LWT - Food Science and Technology 1997, 30(6):602-608.
    • (1997) LWT - Food Science and Technology , vol.30 , Issue.6 , pp. 602-608
    • Gómez-Guillén, M.C.1    Borderías, A.J.2    Montero, P.3
  • 20
    • 78751641604 scopus 로고    scopus 로고
    • The effects of pre-salting methods on water distribution and protein denaturation of dry salted and rehydrated cod-A low-field NMR study
    • Gudjónsdóttir M., Arason S., Rustad T. The effects of pre-salting methods on water distribution and protein denaturation of dry salted and rehydrated cod-A low-field NMR study. Journal of Food Engineering 2011, 104(1):23-29.
    • (2011) Journal of Food Engineering , vol.104 , Issue.1 , pp. 23-29
    • Gudjónsdóttir, M.1    Arason, S.2    Rustad, T.3
  • 21
    • 36448962326 scopus 로고    scopus 로고
    • Raman spectroscopy a promising technique for quality assessment of meat and fish: A review
    • Herrero A.M. Raman spectroscopy a promising technique for quality assessment of meat and fish: A review. Food Chemistry 2008, 107(4):1642-1651.
    • (2008) Food Chemistry , vol.107 , Issue.4 , pp. 1642-1651
    • Herrero, A.M.1
  • 22
    • 0030359675 scopus 로고    scopus 로고
    • Elucidation of interactions of lysozyme with whey proteins by Raman spectroscopy
    • Howell N., Li-Chan E. Elucidation of interactions of lysozyme with whey proteins by Raman spectroscopy. International Journal of Food Science and Technology 1996, 31(5):439-451.
    • (1996) International Journal of Food Science and Technology , vol.31 , Issue.5 , pp. 439-451
    • Howell, N.1    Li-Chan, E.2
  • 23
    • 0032909732 scopus 로고    scopus 로고
    • Raman spectral analysis in the CH stretching region of proteins and amino acids for investigation of hydrophobic interactions
    • Howell N.K., Arteaga G., Nakai S., Li-Chan E.C. Raman spectral analysis in the CH stretching region of proteins and amino acids for investigation of hydrophobic interactions. Journal of Agricultural and Food Chemistry 1999, 47(3):924-933.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.3 , pp. 924-933
    • Howell, N.K.1    Arteaga, G.2    Nakai, S.3    Li-Chan, E.C.4
  • 24
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels
    • Ikeda S., Li-Chan E.C. Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels. Food Hydrocolloids 2004, 18(3):489-498.
    • (2004) Food Hydrocolloids , vol.18 , Issue.3 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.2
  • 25
    • 33745258660 scopus 로고    scopus 로고
    • Quality of reduced-fat frankfurter modified by konjac-starch mixed gels
    • Kao W.T., Lin K.W. Quality of reduced-fat frankfurter modified by konjac-starch mixed gels. Journal of Food Science 2006, 71(4):S326-S332.
    • (2006) Journal of Food Science , vol.71 , Issue.4 , pp. S326-S332
    • Kao, W.T.1    Lin, K.W.2
  • 26
    • 33644551699 scopus 로고
    • Studies on the chemical structure of konjac mannan
    • Kato K., Matsuda K. Studies on the chemical structure of konjac mannan. Agricultural and Biological Chemistry 1969, 33(10):1446-1453.
    • (1969) Agricultural and Biological Chemistry , vol.33 , Issue.10 , pp. 1446-1453
    • Kato, K.1    Matsuda, K.2
  • 27
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Academic Press, New York
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Advances in protein chemistry 1959, Vol. 14:1-64. Academic Press, New York.
    • (1959) Advances in protein chemistry , vol.14 , pp. 1-64
    • Kauzmann, W.1
  • 28
    • 0002351728 scopus 로고
    • Influence of shear treatments on consistency and gelling properties of whey protein isolate suspensions
    • Ker Y.C., Toledo R.T. Influence of shear treatments on consistency and gelling properties of whey protein isolate suspensions. Journal of Food Science 1992, 57(1):82-85.
    • (1992) Journal of Food Science , vol.57 , Issue.1 , pp. 82-85
    • Ker, Y.C.1    Toledo, R.T.2
  • 30
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S., Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advances in Protein Chemistry 1986, 38:181-364.
    • (1986) Advances in Protein Chemistry , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 31
    • 0033630245 scopus 로고    scopus 로고
    • Fish protein hydrolysates: Production, biochemical, and functional properties
    • Kristinsson H.G., Rasco B.A. Fish protein hydrolysates: Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition 2000, 40(1):43-81.
    • (2000) Critical Reviews in Food Science and Nutrition , vol.40 , Issue.1 , pp. 43-81
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0015868654 scopus 로고
    • Detection of changes in the environment of hydrocarbon chains by Raman spectroscopy and its application to lipid-protein systems
    • Larsson K., Rand R.P. Detection of changes in the environment of hydrocarbon chains by Raman spectroscopy and its application to lipid-protein systems. Biochimica et Biophysica Acta - Lipids and Lipid Metabolism 1973, 326(2):245-255.
    • (1973) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.326 , Issue.2 , pp. 245-255
    • Larsson, K.1    Rand, R.P.2
  • 35
    • 0000645205 scopus 로고
    • Ingredient and formulation technology for surimi-based products
    • Lee C.M., Wu M.C., Okada M. Ingredient and formulation technology for surimi-based products. Surimi Technology 1992, 53:273-302.
    • (1992) Surimi Technology , vol.53 , pp. 273-302
    • Lee, C.M.1    Wu, M.C.2    Okada, M.3
  • 36
    • 0036129584 scopus 로고    scopus 로고
    • Thermal gelation of brown trout myofibrils from white and red muscles: Effect of pH and ionic strength
    • Lefevre 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
    • Lefevre, F.1    Fauconneau, B.2    Ouali, A.3    Culioli, J.4
  • 37
    • 84855198886 scopus 로고
    • Diffusion of a globular protein in amylose and amylopectin gels
    • Leloup V.M., Colonna P., Ring S.G. Diffusion of a globular protein in amylose and amylopectin gels. Food Hydrocolloids 1987, 1(5):465-469.
    • (1987) Food Hydrocolloids , vol.1 , Issue.5 , pp. 465-469
    • Leloup, V.M.1    Colonna, P.2    Ring, S.G.3
  • 38
    • 84894320568 scopus 로고    scopus 로고
    • Preparation and characterization of heterogeneous deacetylated konjac glucomannan
    • Li J., Ye T., Wu X., Chen J., Wang S., Lin L., Li B. Preparation and characterization of heterogeneous deacetylated konjac glucomannan. Food Hydrocolloids 2014, 40:9-15.
    • (2014) Food Hydrocolloids , vol.40 , pp. 9-15
    • Li, J.1    Ye, T.2    Wu, X.3    Chen, J.4    Wang, S.5    Lin, L.6    Li, B.7
  • 39
    • 0030295334 scopus 로고    scopus 로고
    • The applications of Raman spectroscopy in food science
    • Li-Chan E.C.Y. The applications of Raman spectroscopy in food science. Trends in Food Science & Technology 1996, 7(11):361-370.
    • (1996) Trends in Food Science & Technology , vol.7 , Issue.11 , pp. 361-370
    • Li-Chan, E.C.Y.1
  • 40
    • 0001684139 scopus 로고
    • Raman spectroscopic study of thermally and/or dithiothreitol induced gelation of lysozyme
    • Li-Chan E., Nakai S. Raman spectroscopic study of thermally and/or dithiothreitol induced gelation of lysozyme. Journal of Agricultural and Food Chemistry 1991, 39(7):1238-1245.
    • (1991) Journal of Agricultural and Food Chemistry , vol.39 , Issue.7 , pp. 1238-1245
    • Li-Chan, E.1    Nakai, S.2
  • 42
    • 79952536911 scopus 로고    scopus 로고
    • Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties
    • Liu R., Zhao S.M., Xie B.J., Xiong S.B. Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties. Food Hydrocolloids 2011, 25(5):898-906.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 898-906
    • Liu, R.1    Zhao, S.M.2    Xie, B.J.3    Xiong, S.B.4
  • 43
    • 84873920513 scopus 로고    scopus 로고
    • Influence of konjac glucomannan on gelling properties and water state in egg white protein gel
    • Liu J., Zhu K., Ye T., Wan S., Wang Y., Wang D., Wang C. Influence of konjac glucomannan on gelling properties and water state in egg white protein gel. Food Research International 2013, 51(2):437-443.
    • (2013) Food Research International , vol.51 , Issue.2 , pp. 437-443
    • Liu, J.1    Zhu, K.2    Ye, T.3    Wan, S.4    Wang, Y.5    Wang, D.6    Wang, C.7
  • 44
    • 77950065206 scopus 로고    scopus 로고
    • Thermal inactivation and growth potential of Listeria innocua in rehydrated salt-cured cod prepared for ready-to-eat products
    • Lorentzen G., Ytterstad E., Olsen R.L., Skjerdal T. Thermal inactivation and growth potential of Listeria innocua in rehydrated salt-cured cod prepared for ready-to-eat products. Food Control 2010, 21(8):1121-1126.
    • (2010) Food Control , vol.21 , Issue.8 , pp. 1121-1126
    • Lorentzen, G.1    Ytterstad, E.2    Olsen, R.L.3    Skjerdal, T.4
  • 46
  • 47
    • 84892608100 scopus 로고    scopus 로고
    • Curcumin-β-cyclodextrin inclusion complex: Stability, solubility, characterisation by FT-IR, FT-Raman, X-ray diffraction and photoacoustic spectroscopy, and food application
    • Mangolim C.S., Moriwaki C., Nogueira A.C., Sato F., Baesso M.L., Neto A.M., Matioli G. Curcumin-β-cyclodextrin inclusion complex: Stability, solubility, characterisation by FT-IR, FT-Raman, X-ray diffraction and photoacoustic spectroscopy, and food application. Food Chemistry 2014, 153:361-370.
    • (2014) Food Chemistry , vol.153 , pp. 361-370
    • Mangolim, C.S.1    Moriwaki, C.2    Nogueira, A.C.3    Sato, F.4    Baesso, M.L.5    Neto, A.M.6    Matioli, G.7
  • 48
    • 6344277284 scopus 로고    scopus 로고
    • Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution
    • Ngarize S., Herman H., Adams A., Howell N. Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. Journal of Agricultural and Food Chemistry 2004, 52(21):6470-6477.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.21 , pp. 6470-6477
    • Ngarize, S.1    Herman, H.2    Adams, A.3    Howell, N.4
  • 49
    • 84891025776 scopus 로고    scopus 로고
    • Ovalbumin-gum Arabic interactions: Effect of pH, temperature, salt, biopolymers ratio and total concentration
    • Niu F., Su Y., Liu Y., Wang G., Zhang Y., Yang Y. Ovalbumin-gum Arabic interactions: Effect of pH, temperature, salt, biopolymers ratio and total concentration. Colloids and Surfaces B: Biointerfaces 2014, 113:477-482.
    • (2014) Colloids and Surfaces B: Biointerfaces , vol.113 , pp. 477-482
    • Niu, F.1    Su, Y.2    Liu, Y.3    Wang, G.4    Zhang, Y.5    Yang, Y.6
  • 50
    • 0001393486 scopus 로고
    • Raman spectroscopic study of thermally induced gelation of whey proteins
    • Nonaka M., Li-Chan E., Nakai S. Raman spectroscopic study of thermally induced gelation of whey proteins. Journal of Agricultural and Food Chemistry 1993, 41(8):1176-1181.
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , Issue.8 , pp. 1176-1181
    • Nonaka, M.1    Li-Chan, E.2    Nakai, S.3
  • 52
    • 0000550613 scopus 로고    scopus 로고
    • Ingredient technology and formulation development
    • Marcel Dekker, New York, NY, J.W. Park (Ed.)
    • Park J.W. Ingredient technology and formulation development. Surimi and surimi seafood 2000, 343-391. Marcel Dekker, New York, NY. J.W. Park (Ed.).
    • (2000) Surimi and surimi seafood , pp. 343-391
    • Park, J.W.1
  • 53
    • 16744366516 scopus 로고    scopus 로고
    • Fish myosin aggregation as affected by freezing and initial physical state
    • Ramiarez J.A., Martian-Polo M.O., Bandman E. Fish myosin aggregation as affected by freezing and initial physical state. Journal of Food Science 2000, 65(4):556-560.
    • (2000) Journal of Food Science , vol.65 , Issue.4 , pp. 556-560
    • Ramiarez, J.A.1    Martian-Polo, M.O.2    Bandman, E.3
  • 54
    • 0036132845 scopus 로고    scopus 로고
    • Effect of xanthan and locust bean gums on the gelling properties of myofibrillar protein
    • Ramírez J.A., Barrera M., Morales O.G., Vázquez M. Effect of xanthan and locust bean gums on the gelling properties of myofibrillar protein. Food Hydrocolloids 2002, 16(1):11-16.
    • (2002) Food Hydrocolloids , vol.16 , Issue.1 , pp. 11-16
    • Ramírez, J.A.1    Barrera, M.2    Morales, O.G.3    Vázquez, M.4
  • 55
    • 79961024283 scopus 로고    scopus 로고
    • Food hydrocolloids as additives to improve the mechanical and functional properties of fish products: A review
    • Ramírez J.A., Uresti R.M., Velazquez G., Vázquez M. Food hydrocolloids as additives to improve the mechanical and functional properties of fish products: A review. Food Hydrocolloids 2011, 25(8):1842-1852.
    • (2011) Food Hydrocolloids , vol.25 , Issue.8 , pp. 1842-1852
    • Ramírez, J.A.1    Uresti, R.M.2    Velazquez, G.3    Vázquez, M.4
  • 60
    • 0019673237 scopus 로고
    • Adhesion and cohesion. Protein functionality in foods
    • American Chemical Society, Washington, DC, (Chapter 6), J.P. Cherry (Ed.)
    • Wall J.S., Huebner F.R. Adhesion and cohesion. Protein functionality in foods. ACS symposium series 147 1981, 111-130. American Chemical Society, Washington, DC, (Chapter 6). J.P. Cherry (Ed.).
    • (1981) ACS symposium series 147 , pp. 111-130
    • Wall, J.S.1    Huebner, F.R.2
  • 61
    • 33751499115 scopus 로고
    • Thermal gelation of globular proteins: Influence of protein conformation on gel strength
    • Wang C.H., Damodaran S. Thermal gelation of globular proteins: Influence of protein conformation on gel strength. Journal of Agricultural and Food Chemistry 1991, 39(3):433-438.
    • (1991) Journal of Agricultural and Food Chemistry , vol.39 , Issue.3 , pp. 433-438
    • Wang, C.H.1    Damodaran, S.2
  • 62
    • 30844443746 scopus 로고    scopus 로고
    • Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation
    • Westphalen A.D., Briggs J.L., Lonergan S.M. Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation. Meat Science 2006, 72(4):697-703.
    • (2006) Meat Science , vol.72 , Issue.4 , pp. 697-703
    • Westphalen, A.D.1    Briggs, J.L.2    Lonergan, S.M.3
  • 63
    • 67349126511 scopus 로고    scopus 로고
    • Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella)
    • Xiong G., Cheng W., Ye L., Du X., Zhou M., Lin R., et al. Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella). Food Chemistry 2009, 116(2):413-418.
    • (2009) Food Chemistry , vol.116 , Issue.2 , pp. 413-418
    • Xiong, G.1    Cheng, W.2    Ye, L.3    Du, X.4    Zhou, M.5    Lin, R.6
  • 64
    • 78649918829 scopus 로고    scopus 로고
    • Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic
    • Xu X.L., Han M.Y., Fei Y., Zhou G.H. Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic. Meat Science 2011, 87(3):159-164.
    • (2011) Meat Science , vol.87 , Issue.3 , pp. 159-164
    • Xu, X.L.1    Han, M.Y.2    Fei, Y.3    Zhou, G.H.4
  • 66
    • 84886247182 scopus 로고    scopus 로고
    • High pressure homogenization to improve the stability of casein-hydroxypropyl cellulose aqueous systems
    • Ye R., Harte F. High pressure homogenization to improve the stability of casein-hydroxypropyl cellulose aqueous systems. Food Hydrocolloids 2014, 35:670-677.
    • (2014) Food Hydrocolloids , vol.35 , pp. 670-677
    • Ye, R.1    Harte, F.2
  • 67
    • 84908502281 scopus 로고    scopus 로고
    • Effects of deacetylation of konjac glucomannan on Alaska Pollock surimi gels subjected to high-temperature (120 °C) treatment
    • Zhang T., Xue Y., Li Z., Wang Y., Xue C. Effects of deacetylation of konjac glucomannan on Alaska Pollock surimi gels subjected to high-temperature (120 °C) treatment. Food Hydrocolloids 2015, 43:125-131.
    • (2015) Food Hydrocolloids , vol.43 , pp. 125-131
    • Zhang, T.1    Xue, Y.2    Li, Z.3    Wang, Y.4    Xue, C.5
  • 68
    • 84869488634 scopus 로고    scopus 로고
    • Effects of high-temperature treatment (≥100 °C) on Alaska Pollock (Theragra chalcogramma) surimi gels
    • Zhang L., Xue Y., Xu J., Li Z., Xue C. Effects of high-temperature treatment (≥100 °C) on Alaska Pollock (Theragra chalcogramma) surimi gels. Journal of Food Engineering 2013, 115(1):115-120.
    • (2013) Journal of Food Engineering , vol.115 , Issue.1 , pp. 115-120
    • Zhang, L.1    Xue, Y.2    Xu, J.3    Li, Z.4    Xue, C.5


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