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Volumn 23, Issue 5, 2014, Pages 1417-1423

Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels

Author keywords

fibrils; gels structure; rice bran protein; solutions viscosity

Indexed keywords

ATOMIC FORCE MICROSCOPY; AZO DYES; COMPLEX NETWORKS; DICHROISM; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; PHYSICOCHEMICAL PROPERTIES; PROTEINS; SCANNING ELECTRON MICROSCOPY; SHEAR STRESS; SHEAR THINNING; SPECTRUM ANALYSIS;

EID: 84918546220     PISSN: 12267708     EISSN: 20926456     Source Type: Journal    
DOI: 10.1007/s10068-014-0194-1     Document Type: Article
Times cited : (46)

References (32)
  • 2
    • 48849103441 scopus 로고    scopus 로고
    • Properties of protein fibrils in whey protein isolate solutions: Microstructure, flow behaviour and gelation
    • COI: 1:CAS:528:DC%2BD1cXhtVSjsrnN
    • Akkermans C, Goot AJ, Venem P, Linden E, Remko MB. Properties of protein fibrils in whey protein isolate solutions: Microstructure, flow behaviour and gelation. Int. Dent. J. 18: 1034–1042 (2008)
    • (2008) Int. Dent. J. , vol.18 , pp. 1034-1042
    • Akkermans, C.1    Goot, A.J.2    Venem, P.3    Linden, E.4    Remko, M.B.5
  • 3
    • 34047132881 scopus 로고    scopus 로고
    • Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study
    • Stephen RE, Saif UR, Geoffrey C. Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study. Food Hydrocolloid. 21: 1081–1091 (2007)
    • (2007) Food Hydrocolloid. , vol.21 , pp. 1081-1091
    • Stephen, R.E.1    Saif, U.R.2    Geoffrey, C.3
  • 4
    • 84873892393 scopus 로고    scopus 로고
    • Heat-induced fibril assembly of vicilin at pH 2.0: Reaction kinetics, influence of ionic strength and protein concentration, and molecular mechanism
    • COI: 1:CAS:528:DC%2BC3sXlvVCks7c%3D
    • Liu J, Tang CH. Heat-induced fibril assembly of vicilin at pH 2.0: Reaction kinetics, influence of ionic strength and protein concentration, and molecular mechanism. Food Res. Int. 51: 621–632 (2013)
    • (2013) Food Res. Int. , vol.51 , pp. 621-632
    • Liu, J.1    Tang, C.H.2
  • 5
    • 84888072817 scopus 로고    scopus 로고
    • The effect of limited proteolysis by different proteases on the formation of whey protein fibrils
    • COI: 1:CAS:528:DC%2BC3sXhs1WisbbJ
    • Gao YZ, Xu HH, Ju TT, Zhao XH. The effect of limited proteolysis by different proteases on the formation of whey protein fibrils. J. Dairy. Sci. 96: 7383–7392 (2013)
    • (2013) J. Dairy. Sci. , vol.96 , pp. 7383-7392
    • Gao, Y.Z.1    Xu, H.H.2    Ju, T.T.3    Zhao, X.H.4
  • 6
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea
    • COI: 1:CAS:528:DC%2BD38XntlCrtrw%3D
    • Hamada D, Dobson CM. A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11: 2417–2426 (2002)
    • (2002) Protein Sci. , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 8
    • 34147155531 scopus 로고    scopus 로고
    • Effect of enzymatic hydrolysis of 7S globulin, a soybean protein, on its allergenicity and identification of its allergenic hydrolyzed fragments using SDS-PAGE
    • COI: 1:CAS:528:DC%2BD28XjtFejtbw%3D
    • Keum EH, Lee SI, Oh SS. Effect of enzymatic hydrolysis of 7S globulin, a soybean protein, on its allergenicity and identification of its allergenic hydrolyzed fragments using SDS-PAGE. Food Sci. Biotechnol. 15: 128–132 (2006)
    • (2006) Food Sci. Biotechnol. , vol.15 , pp. 128-132
    • Keum, E.H.1    Lee, S.I.2    Oh, S.S.3
  • 9
    • 34347351399 scopus 로고    scopus 로고
    • Self-assembling peptide inspired by a barnacle underwater adhesive protein
    • COI: 1:CAS:528:DC%2BD2sXls1Smtb0%3D
    • Nakano M, Shen JR, Kamino K. Self-assembling peptide inspired by a barnacle underwater adhesive protein. Biomacromolecules 8: 1830–1835 (2007)
    • (2007) Biomacromolecules , vol.8 , pp. 1830-1835
    • Nakano, M.1    Shen, J.R.2    Kamino, K.3
  • 10
    • 77955919239 scopus 로고    scopus 로고
    • The impact of concentration, temperature and pH on dynamic rheology of psyllium gels
    • COI: 1:CAS:528:DC%2BC3cXpslOltLw%3D
    • Farahnaky A, Askari H, Majzoobi M, Mesbahi G. The impact of concentration, temperature and pH on dynamic rheology of psyllium gels. J. Food Eng. 100: 294–301 (2010)
    • (2010) J. Food Eng. , vol.100 , pp. 294-301
    • Farahnaky, A.1    Askari, H.2    Majzoobi, M.3    Mesbahi, G.4
  • 12
    • 75149122292 scopus 로고    scopus 로고
    • Thermal aggregation and gelation of kidney bean (Phaseolus vulgaris L.) protein isolate at pH 2.0: Influence of ionic strength
    • Zhang YH, Tang CH, Wen QB, Yang XQ, Li L, Deng WL. Thermal aggregation and gelation of kidney bean (Phaseolus vulgaris L.) protein isolate at pH 2.0: Influence of ionic strength. Food Hydrocolloid. 24: 266–274 (2010)
    • (2010) Food Hydrocolloid. , vol.24 , pp. 266-274
    • Zhang, Y.H.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4    Li, L.5    Deng, W.L.6
  • 13
    • 34249989050 scopus 로고    scopus 로고
    • Influence of pH and NaCl on rheological properties of rennet-induced casein gels made from UF concentrated skim milk
    • COI: 1:CAS:528:DC%2BD2sXmsFKmsLY%3D
    • Karlsson AO, Ipsen R, Ardo Y. Influence of pH and NaCl on rheological properties of rennet-induced casein gels made from UF concentrated skim milk. Int. Dairy J. 17: 1053–1062 (2007)
    • (2007) Int. Dairy J. , vol.17 , pp. 1053-1062
    • Karlsson, A.O.1    Ipsen, R.2    Ardo, Y.3
  • 14
    • 67349160258 scopus 로고    scopus 로고
    • Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates
    • COI: 1:CAS:528:DC%2BD1MXms12iurc%3D
    • Chanput W, Theerakulkait C, Nakai S. Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates. J. Cereal Sci. 49: 422–428 (2009)
    • (2009) J. Cereal Sci. , vol.49 , pp. 422-428
    • Chanput, W.1    Theerakulkait, C.2    Nakai, S.3
  • 15
    • 37049122099 scopus 로고
    • The use of automation in determining nitrogen by the Kjeldahl method, with final calculations by computer
    • COI: 1:CAS:528:DyaE3cXhtVOlu74%3D
    • Davidson J, Mathieson J, Boyne AW. The use of automation in determining nitrogen by the Kjeldahl method, with final calculations by computer. Analyst 95: 181–193 (1970)
    • (1970) Analyst , vol.95 , pp. 181-193
    • Davidson, J.1    Mathieson, J.2    Boyne, A.W.3
  • 16
    • 77954552574 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from kidney bean 7S globulin (Phaseolin) at pH 2.0
    • COI: 1:CAS:528:DC%2BC3cXnt1CmtrY%3D
    • Tang CH, Zhang YH, Wen QB, Huang QR. Formation of amyloid fibrils from kidney bean 7S globulin (Phaseolin) at pH 2.0. J. Agr. Food Chem. 58: 8061–8068 (2010)
    • (2010) J. Agr. Food Chem. , vol.58 , pp. 8061-8068
    • Tang, C.H.1    Zhang, Y.H.2    Wen, Q.B.3    Huang, Q.R.4
  • 17
    • 0036177818 scopus 로고    scopus 로고
    • Rheology and structure of ovalbumin gels at low pH and low ionic strength
    • COI: 1:CAS:528:DC%2BD38XhtlSku7g%3D
    • Weijers M, Sagis LMC, Veerman C, Sperber B, van der Linden E. Rheology and structure of ovalbumin gels at low pH and low ionic strength. Food Hydrocolloid. 16: 269–276 (2002)
    • (2002) Food Hydrocolloid. , vol.16 , pp. 269-276
    • Weijers, M.1    Sagis, L.M.C.2    Veerman, C.3    Sperber, B.4    van der Linden, E.5
  • 18
    • 80054996044 scopus 로고    scopus 로고
    • β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions
    • COI: 1:CAS:528:DC%2BC3MXhtlGiu7%2FF
    • Loveday SM, Wang XL, Rao MA, Anema SG, Singh H. β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions. Food Hydrocolloid. 27: 242–249 (2012)
    • (2012) Food Hydrocolloid. , vol.27 , pp. 242-249
    • Loveday, S.M.1    Wang, X.L.2    Rao, M.A.3    Anema, S.G.4    Singh, H.5
  • 19
    • 84862794715 scopus 로고    scopus 로고
    • Improvement of heat-induced fibril assembly of soy β-conglycinin (7S Globulins) at pH 2.0 through electrostatic screening
    • COI: 1:CAS:528:DC%2BC38XjsVWgtro%3D
    • Tang CH, Wang SS, Huang QR. Improvement of heat-induced fibril assembly of soy β-conglycinin (7S Globulins) at pH 2.0 through electrostatic screening. Food Res. Int. 46: 229–236 (2012)
    • (2012) Food Res. Int. , vol.46 , pp. 229-236
    • Tang, C.H.1    Wang, S.S.2    Huang, Q.R.3
  • 21
    • 43649090986 scopus 로고    scopus 로고
    • Formation of amyloid fibrils by bovine carbonic anhydrase
    • COI: 1:CAS:528:DC%2BD1cXmt1Oit7k%3D
    • Rana A, Gupta TP, Bansal S, Kundu B. Formation of amyloid fibrils by bovine carbonic anhydrase. Biochim. Biophys. Acta 1784: 930–35 (2008)
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 930-935
    • Rana, A.1    Gupta, T.P.2    Bansal, S.3    Kundu, B.4
  • 22
    • 3343003514 scopus 로고    scopus 로고
    • Nilsson. Techniques to study amyloid fibril formation in vitro
    • Melanie R. Nilsson. Techniques to study amyloid fibril formation in vitro. Methods 34: 151–160 (2004)
    • (2004) Methods , vol.34 , pp. 151-160
    • Melanie, R.1
  • 23
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • Martino C, Fabrizio C, Christopher MD. Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys. J. 89: 4201–4210 (2005)
    • (2005) Biophys. J. , vol.89 , pp. 4201-4210
    • Martino, C.1    Fabrizio, C.2    Christopher, M.D.3
  • 24
    • 48749116996 scopus 로고    scopus 로고
    • Appraisal of casein’s inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis
    • COI: 1:CAS:528:DC%2BD1cXpslWls70%3D
    • Khodarahmi R, Beyrami M, Soori H. Appraisal of casein’s inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis. Arch. Biochem. Biophys. 477: 67–76 (2008)
    • (2008) Arch. Biochem. Biophys. , vol.477 , pp. 67-76
    • Khodarahmi, R.1    Beyrami, M.2    Soori, H.3
  • 25
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • COI: 1:CAS:528:DyaK2sXhslOmsLs%3D
    • Kelly SM, Price NC. The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta 1338: 161–185 (1997)
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 26
    • 34047234694 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing
    • COI: 1:CAS:528:DC%2BD28XhtlWmu7zK
    • Pearce FG, Mackintosh SH, Gerrard JA. Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing. J. Agr. Food Chem. 55: 318–322 (2007)
    • (2007) J. Agr. Food Chem. , vol.55 , pp. 318-322
    • Pearce, F.G.1    Mackintosh, S.H.2    Gerrard, J.A.3
  • 27
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Narasimha S, Robert W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287: 252–260 (2000)
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Narasimha, S.1    Robert, W.2
  • 29
    • 84886406532 scopus 로고    scopus 로고
    • New parameters for the examination of the pectin gelation process
    • Kastner H, Einhorn SU, Senge B. New parameters for the examination of the pectin gelation process. Roy. Soc. Ch. 16: 191–197 (2012)
    • (2012) Roy. Soc. Ch. , vol.16 , pp. 191-197
    • Kastner, H.1    Einhorn, S.U.2    Senge, B.3
  • 30
    • 79151470587 scopus 로고    scopus 로고
    • Effects of rice bran fiber on heat-induced gel prepared with pork salt-soluble meat proteins in model system
    • COI: 1:CAS:528:DC%2BC3MXht1Cgu78%3D
    • Choi YS, Choi JH, Han DJ, Kim HY, Lee MA, Kim HW, Jeong JY, Kim CJ. Effects of rice bran fiber on heat-induced gel prepared with pork salt-soluble meat proteins in model system. Meat Sci. 88: 59–66 (2011)
    • (2011) Meat Sci. , vol.88 , pp. 59-66
    • Choi, Y.S.1    Choi, J.H.2    Han, D.J.3    Kim, H.Y.4    Lee, M.A.5    Kim, H.W.6    Jeong, J.Y.7    Kim, C.J.8
  • 31
    • 0036810087 scopus 로고    scopus 로고
    • Effect of ionic strength on rinsing and alkaline cleaning of ultrafiltration inorganic membranes fouled with whey proteins
    • COI: 1:CAS:528:DC%2BD38XmvVWktLY%3D
    • Matzinos P, Álvarez R. Effect of ionic strength on rinsing and alkaline cleaning of ultrafiltration inorganic membranes fouled with whey proteins. J. Membrane Sci. 208: 23–30 (2002)
    • (2002) J. Membrane Sci. , vol.208 , pp. 23-30
    • Matzinos, P.1    Álvarez, R.2
  • 32
    • 71649098478 scopus 로고    scopus 로고
    • Effects of pH and ionic strength on the rheology and microstructure of a pressure-induced whey protein gel
    • COI: 1:CAS:528:DC%2BD1MXhsVymtbvN
    • He JS, Azuma N, Yang HW. Effects of pH and ionic strength on the rheology and microstructure of a pressure-induced whey protein gel. Int. Dairy J. 20: 89–95 (2010)
    • (2010) Int. Dairy J. , vol.20 , pp. 89-95
    • He, J.S.1    Azuma, N.2    Yang, H.W.3


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