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Volumn 54, Issue 12, 2006, Pages 4198-4207

Alteration of kafirin and kafirin film structure by heating with microwave energy and tannin complexation

Author keywords

Bioplastic films; Disulfide bonds; FTIR; Kafirin; Microwave energy; Protein secondary structure; Raman; SDS PAGE; Tannins

Indexed keywords

KAFIRIN PROTEIN, SORGHUM BICOLOR; TANNIN DERIVATIVE; VEGETABLE PROTEIN;

EID: 33745754513     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf052942z     Document Type: Article
Times cited : (47)

References (40)
  • 1
    • 0030771479 scopus 로고    scopus 로고
    • Films from laboratory-extracted sorghum kafirin
    • Buffo, R. A.; Weller, C. L.; Gennadios, A. Films from laboratory-extracted sorghum kafirin. Cereal Chem. 1997, 74, 473-475.
    • (1997) Cereal Chem. , vol.74 , pp. 473-475
    • Buffo, R.A.1    Weller, C.L.2    Gennadios, A.3
  • 2
    • 8144225904 scopus 로고    scopus 로고
    • Sorghum kafirin film property modification with hydrolyzable and condensed tannins
    • Emmambux, M. N.; Stading, M.; Taylor, J. R. N. Sorghum kafirin film property modification with hydrolyzable and condensed tannins. J. Cereal Sci. 2004, 40, 127-135.
    • (2004) J. Cereal Sci. , vol.40 , pp. 127-135
    • Emmambux, M.N.1    Stading, M.2    Taylor, J.R.N.3
  • 3
    • 24744470954 scopus 로고    scopus 로고
    • Effect of microwave heating of kafirin on the functional properties of kafirin films
    • Byaruhanga, Y. B.; Erasmus, C.; Taylor, J. R. N. Effect of microwave heating of kafirin on the functional properties of kafirin films. Cereal Chem. 2005, 82, 565-573.
    • (2005) Cereal Chem. , vol.82 , pp. 565-573
    • Byaruhanga, Y.B.1    Erasmus, C.2    Taylor, J.R.N.3
  • 4
    • 0037380601 scopus 로고    scopus 로고
    • Sorghum kafirin interaction with various phenolic compounds
    • Emmambux, M. N.; Taylor, J. R. N. Sorghum kafirin interaction with various phenolic compounds. J. Sci. Food Agric. 2003, 83, 402-407.
    • (2003) J. Sci. Food Agric. , vol.83 , pp. 402-407
    • Emmambux, M.N.1    Taylor, J.R.N.2
  • 7
    • 0036139680 scopus 로고    scopus 로고
    • Zein: A history of processing and use
    • Lawton, J. W. Zein: A history of processing and use. Cereal Chem. 2002, 79, 1-18.
    • (2002) Cereal Chem. , vol.79 , pp. 1-18
    • Lawton, J.W.1
  • 8
    • 0000898564 scopus 로고
    • Characterization of the kafirin gene family from sorghum reveals extensive homology with zein from maize
    • DeRose, R. T.; Ma, D. P.; Kwon, I. S.; Hasnain, S. E.; Klassy, R. C.; Hall, T. C. Characterization of the kafirin gene family from sorghum reveals extensive homology with zein from maize. Plant Mol. Biol. 1989, 10, 245-256.
    • (1989) Plant Mol. Biol. , vol.10 , pp. 245-256
    • DeRose, R.T.1    Ma, D.P.2    Kwon, I.S.3    Hasnain, S.E.4    Klassy, R.C.5    Hall, T.C.6
  • 9
  • 10
    • 0001141868 scopus 로고    scopus 로고
    • Characterisation of sorghum kafirins in relation to their cross-linking behaviour
    • El Nour, I. N. A.; Peruffo, A. D. B.; Curioni, A. Characterisation of sorghum kafirins in relation to their cross-linking behaviour. J. Cereal Sci. 1998, 28, 197-207.
    • (1998) J. Cereal Sci. , vol.28 , pp. 197-207
    • El Nour, I.N.A.1    Peruffo, A.D.B.2    Curioni, A.3
  • 11
    • 0034563010 scopus 로고    scopus 로고
    • Microwave heating and γ-irradiation treatment of rapeseed (Brassica napus)
    • Valentova, O.; Novotina, Z.; Svoboda, Z.; Schwarz, W.; Kas, J. Microwave heating and γ-irradiation treatment of rapeseed (Brassica napus). J. Food Lipids 2000, 7, 237-245.
    • (2000) J. Food Lipids , vol.7 , pp. 237-245
    • Valentova, O.1    Novotina, Z.2    Svoboda, Z.3    Schwarz, W.4    Kas, J.5
  • 12
    • 0034940857 scopus 로고    scopus 로고
    • Electrophoretic patterns of microwaved and γ-irradiated beef liver proteins
    • Farag, R. S.; Hegazy, R. A.; El-Khawas, K. H.; Farag, M. M. Electrophoretic patterns of microwaved and γ-irradiated beef liver proteins. J. Sci. Food Agric. 2001, 81, 975-982.
    • (2001) J. Sci. Food Agric. , vol.81 , pp. 975-982
    • Farag, R.S.1    Hegazy, R.A.2    El-Khawas, K.H.3    Farag, M.M.4
  • 14
    • 1842430710 scopus 로고    scopus 로고
    • Sequential in vitro pepsin digestion of uncooked and cooked sorghum and maize samples
    • Nunes, A.; Correia, I.; Barros, A.; Delgadillo, I. Sequential in vitro pepsin digestion of uncooked and cooked sorghum and maize samples. J. Agric. Food Chem. 2004, 52, 2052-2058.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 2052-2058
    • Nunes, A.1    Correia, I.2    Barros, A.3    Delgadillo, I.4
  • 17
    • 0141813702 scopus 로고    scopus 로고
    • Role of covalent and noncovalent interactions in the formation of films from unheated whey protein solutions following pH adjustment
    • Quinn, G.; Monahan, F. J.; O'Riordan, E. D.; O'Sullivan, M.; Longares, A. Role of covalent and noncovalent interactions in the formation of films from unheated whey protein solutions following pH adjustment. J. Food Sci. 2003, 68, 2284-2288.
    • (2003) J. Food Sci. , vol.68 , pp. 2284-2288
    • Quinn, G.1    Monahan, F.J.2    O'Riordan, E.D.3    O'Sullivan, M.4    Longares, A.5
  • 18
    • 0342963509 scopus 로고
    • Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate
    • Shimada, K.; Cheftel, J. C. Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate. J. Agric. Food Chem. 1988, 36, 147-153.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 147-153
    • Shimada, K.1    Cheftel, J.C.2
  • 19
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey isolate
    • Shimada, K.; Cheftel, J. C. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey isolate. J. Agric. Food Chem. 1989, 37, 161-168.
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 20
    • 0002762455 scopus 로고
    • Heat induced changes in the proteins of whey protein concentrate
    • Li-Chan, E. Heat induced changes in the proteins of whey protein concentrate. J. Food Sci. 1983, 48, 47-56.
    • (1983) J. Food Sci. , vol.48 , pp. 47-56
    • Li-Chan, E.1
  • 21
    • 0141625670 scopus 로고    scopus 로고
    • Evaluation of a sulphydryl-disulphide exchange index (SEI) for whey proteins: β-lactoglobulin and bovine serum albumin
    • Owusu-Apenten, R. K.; Chee, C.; Hwee, O. P. Evaluation of a sulphydryl-disulphide exchange index (SEI) for whey proteins: β-lactoglobulin and bovine serum albumin. Food Chem. 2003, 83, 541-545.
    • (2003) Food Chem. , vol.83 , pp. 541-545
    • Owusu-Apenten, R.K.1    Chee, C.2    Hwee, O.P.3
  • 22
    • 0034004133 scopus 로고    scopus 로고
    • Protein insolubilization and thiol oxidation in sulfite treated wheat gluten films during aging at various temperatures and relative humidities
    • Morel, M.-H.; Bonicel, J.; Micard, V.; Guilbert, S. Protein insolubilization and thiol oxidation in sulfite treated wheat gluten films during aging at various temperatures and relative humidities. J. Agric. Food Chem. 2000, 48, 186-192.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 186-192
    • Morel, M.-H.1    Bonicel, J.2    Micard, V.3    Guilbert, S.4
  • 23
    • 0003081480 scopus 로고
    • Direct colorimetric assay of free thiol groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins
    • Chan, K.-Y.; Wasserman, B. P. Direct colorimetric assay of free thiol groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins. Cereal Chem. 1993, 70, 22-26.
    • (1993) Cereal Chem. , vol.70 , pp. 22-26
    • Chan, K.-Y.1    Wasserman, B.P.2
  • 25
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz, W. K.; Mantsch, H. H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 1988, 952, 115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 26
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Bandekar, J. Amide modes and protein conformation. Biochim. Biophys. Acta 1992, 1120, 123-143.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 28
    • 0042415651 scopus 로고    scopus 로고
    • Basic aspects of the technique and applications of infrared spectroscopy of peptides and proteins
    • Singh, B. R., Ed.; American Chemical Society Symposium Series; American Chemical Society: Washington, DC
    • Singh, B. R. Basic aspects of the technique and applications of infrared spectroscopy of peptides and proteins. In Infrared Analysis of Peptides and Proteins, Principles and Application; Singh, B. R., Ed.; American Chemical Society Symposium Series; American Chemical Society: Washington, DC, 2000; pp 2-37.
    • (2000) Infrared Analysis of Peptides and Proteins, Principles and Application , pp. 2-37
    • Singh, B.R.1
  • 29
    • 0345578674 scopus 로고    scopus 로고
    • Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length
    • Feeney, K. A.; Wellner, N.; Gilbert, S. M.; Halford, N. G.; Tatham, A. S.; Shewry, P. R.; Belton, P. S. Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length. Biopolymers 2003, 72, 123-131.
    • (2003) Biopolymers , vol.72 , pp. 123-131
    • Feeney, K.A.1    Wellner, N.2    Gilbert, S.M.3    Halford, N.G.4    Tatham, A.S.5    Shewry, P.R.6    Belton, P.S.7
  • 30
    • 0033667559 scopus 로고    scopus 로고
    • Insight into protein structure and protein ligand recognition by Fourier transform infrared spectroscopy
    • Jung, J. Insight into protein structure and protein ligand recognition by Fourier transform infrared spectroscopy. J. Mol. Recognit. 2000, 13, 325-351.
    • (2000) J. Mol. Recognit. , vol.13 , pp. 325-351
    • Jung, J.1
  • 31
    • 0041413204 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of peptides: Potentials and pitfalls
    • Singh, B. R., Ed.; American Chemical Society Symposium Series; American Chemical Society: Washington, DC
    • Haris, P. I. Fourier transform infrared spectroscopic studies of peptides: Potentials and pitfalls. In Infrared Analysis of Peptides and Proteins, Principles and Application; Singh, B. R., Ed.; American Chemical Society Symposium Series; American Chemical Society: Washington, DC, 2000; pp 54-95.
    • (2000) Infrared Analysis of Peptides and Proteins, Principles and Application , pp. 54-95
    • Haris, P.I.1
  • 32
    • 0034852941 scopus 로고    scopus 로고
    • Study of oat globulin conformation by Fourier transform infrared spectroscopy
    • Ma, C. Y.; Rout, M. K.; Mock, W. Y. Study of oat globulin conformation by Fourier transform infrared spectroscopy. J. Agric. Food Chem. 2001, 49, 3328-3334.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 3328-3334
    • Ma, C.Y.1    Rout, M.K.2    Mock, W.Y.3
  • 33
    • 0032211792 scopus 로고    scopus 로고
    • Molecular basis of film formation from a soybean protein: Comparison between the conformation of glycinin in aqueous solution and in films
    • Subirade, M.; Kelly, I.; Gueguen, J.; Pezolet, M. Molecular basis of film formation from a soybean protein: comparison between the conformation of glycinin in aqueous solution and in films. Int. J. Biol. Macromol. 1998, 23, 241-249.
    • (1998) Int. J. Biol. Macromol. , vol.23 , pp. 241-249
    • Subirade, M.1    Kelly, I.2    Gueguen, J.3    Pezolet, M.4
  • 35
    • 33745763712 scopus 로고
    • Infrared spectroscopy
    • English Language Book Society/Macmillan: Basingstoke, U.K.
    • Kemp, W. Infrared spectroscopy. In Organic Spectroscopy, 2nd ed.; English Language Book Society/Macmillan: Basingstoke, U.K., 1987; pp 12-81.
    • (1987) Organic Spectroscopy, 2nd Ed. , pp. 12-81
    • Kemp, W.1
  • 36
    • 0036882558 scopus 로고    scopus 로고
    • Vibrational analysis of substituted phenols, Part I, vibrational spectra, normal coordinate analysis and transferability of force constants of some formyl, methoxy-, formylmethoxy-, methyl- and halogeno-phenols
    • Rao, P. V. R.; Rao, G. R. Vibrational analysis of substituted phenols, Part I, vibrational spectra, normal coordinate analysis and transferability of force constants of some formyl, methoxy-, formylmethoxy-, methyl- and halogeno-phenols. Spectrochim. Acta, Part A 2002, 58, 3039-3065.
    • (2002) Spectrochim. Acta, Part A , vol.58 , pp. 3039-3065
    • Rao, P.V.R.1    Rao, G.R.2
  • 37
    • 0032845206 scopus 로고    scopus 로고
    • Removal of phosphorus and organic matter by alum during waste treatment
    • Omoike, A. I.; Vanloon, G. W. Removal of phosphorus and organic matter by alum during waste treatment. Water Res. 1999, 33, 3617-3627.
    • (1999) Water Res. , vol.33 , pp. 3617-3627
    • Omoike, A.I.1    Vanloon, G.W.2
  • 39
    • 0030968136 scopus 로고    scopus 로고
    • Multiple interactions between polyphenols and salivary proline rich protein repeat sequence result in complexation and precipitation
    • Baxter, N. J.; Lilley, T. H.; Haslam, E.; Williamson, M. P. Multiple interactions between polyphenols and salivary proline rich protein repeat sequence result in complexation and precipitation. Biochemistry 1997, 36, 5566-5577.
    • (1997) Biochemistry , vol.36 , pp. 5566-5577
    • Baxter, N.J.1    Lilley, T.H.2    Haslam, E.3    Williamson, M.P.4


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