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Volumn 88, Issue 7, 2011, Pages 1037-1043

Purity assessment of commercial zein products after purification

Author keywords

Circular dichroism; Column filtration; Corn zein; FTIR; Protein purification; SDS PAGE; UV spectral analysis; Visible spectral analysis

Indexed keywords

COLUMN FILTRATION; CORN ZEIN; FTIR; PROTEIN PURIFICATION; SDS-PAGE;

EID: 80051551999     PISSN: 0003021X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11746-011-1765-4     Document Type: Article
Times cited : (25)

References (24)
  • 1
    • 0001034120 scopus 로고
    • Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility
    • 10.1104/pp.80.3.623 1:CAS:528:DyaL28XitVertbg%3D
    • A Esen 1986 Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility Plant Physiol 80 623 627 10.1104/pp.80.3.623 1:CAS:528:DyaL28XitVertbg%3D
    • (1986) Plant Physiol , vol.80 , pp. 623-627
    • Esen, A.1
  • 2
    • 84865232102 scopus 로고    scopus 로고
    • Formation and properties of corn zein films and coatings
    • A. Gennadios (eds). CRC Press Florida
    • Padua GW, Wang Q (2002) Formation and properties of corn zein films and coatings. In: Gennadios A (ed) Protein based films and coatings. CRC Press, Florida, pp 43-67
    • (2002) Protein Based Films and Coatings , pp. 43-67
    • Padua, G.W.1    Wang, Q.2
  • 3
    • 0037777798 scopus 로고    scopus 로고
    • Adhesive properties of corn zein formulation on glass surfaces
    • 10.1021/jf0212183 1:CAS:528:DC%2BD3sXjvFOiur4%3D
    • N Parris L Dickey 2003 Adhesive properties of corn zein formulation on glass surfaces J Agric Food Chem 51 3892 3894 10.1021/jf0212183 1:CAS:528:DC%2BD3sXjvFOiur4%3D
    • (2003) J Agric Food Chem , vol.51 , pp. 3892-3894
    • Parris, N.1    Dickey, L.2
  • 4
    • 51649107639 scopus 로고    scopus 로고
    • Chemistry and physical properties of melt-processed and solution-cross-linked corn zein
    • 10.1021/jf800712k 1:CAS:528:DC%2BD1cXos1ahsrc%3D
    • DJ Sessa A Mohamed JA Byars 2008 Chemistry and physical properties of melt-processed and solution-cross-linked corn zein J Agric Food Chem 56 7067 7075 10.1021/jf800712k 1:CAS:528:DC%2BD1cXos1ahsrc%3D
    • (2008) J Agric Food Chem , vol.56 , pp. 7067-7075
    • Sessa, D.J.1    Mohamed, A.2    Byars, J.A.3
  • 6
    • 43849090166 scopus 로고    scopus 로고
    • Effect of heat on the adsorption capacity of an activated carbon for decolorizing/deodorizing yellow zein
    • 10.1016/j.biortech.2007.11.076 1:CAS:528:DC%2BD1cXmtlCntL0%3D
    • DJ Sessa DE Palmquist 2008 Effect of heat on the adsorption capacity of an activated carbon for decolorizing/deodorizing yellow zein Bioresource Technol 99 6360 6364 10.1016/j.biortech.2007.11.076 1:CAS:528:DC%2BD1cXmtlCntL0%3D
    • (2008) Bioresource Technol , vol.99 , pp. 6360-6364
    • Sessa, D.J.1    Palmquist, D.E.2
  • 7
    • 67349222191 scopus 로고    scopus 로고
    • Decolorization/deodorization of zein via activated carbons and molecular sieves
    • 10.1016/j.indcrop.2008.12.008 1:CAS:528:DC%2BD1MXmtVKjsrg%3D
    • DJ Sessa DE Palmquist 2009 Decolorization/deodorization of zein via activated carbons and molecular sieves Ind Crops Prod 30 162 164 10.1016/j.indcrop.2008.12.008 1:CAS:528:DC%2BD1MXmtVKjsrg%3D
    • (2009) Ind Crops Prod , vol.30 , pp. 162-164
    • Sessa, D.J.1    Palmquist, D.E.2
  • 9
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • 10.2174/1389203003381315 1:CAS:528:DC%2BD3MXns1ehtw%3D%3D
    • SM Kelly NC Price 2000 The use of circular dichroism in the investigation of protein structure and function Current Protein Peptide Sci 1 349 384 10.2174/1389203003381315 1:CAS:528:DC%2BD3MXns1ehtw%3D%3D
    • (2000) Current Protein Peptide Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 11
    • 0242527241 scopus 로고    scopus 로고
    • Conformation of α Zeins in Solid State by Fourier Transform IR
    • DOI 10.1002/bip.10481
    • LA Forato T Bicudo LA Colnago 2003 Conformation of α zeins in solid state by Fourier transform IR Biopolymers Biospectrosc Section 72 421 426 10.1002/bip.10481 1:CAS:528:DC%2BD3sXptFWltrc%3D (Pubitemid 37413219)
    • (2003) Biopolymers - Biospectroscopy Section , vol.72 , Issue.6 , pp. 421-426
    • Forato, L.A.1    Bicudo, T.D.C.2    Colnago, L.A.3
  • 13
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • DOI 10.1016/j.bbabio.2007.06.004, PII S0005272807001375
    • A Barth 2007 Infrared spectroscopy of proteins Biochim Biophys Acta 1767 1073 1101 10.1016/j.bbabio.2007.06.004 1:CAS:528:DC%2BD2sXpvFWmt7Y%3D (Pubitemid 47313388)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.9 , pp. 1073-1101
    • Barth, A.1
  • 14
    • 0000463479 scopus 로고
    • Infrared spectroscopy and optical rotary dispersion of zein, wheat gluten and gliadin
    • 10.1021/j150558a014 1:CAS:528:DyaG1cXivVKitA%3D%3D
    • CB Kretschmer 1957 Infrared spectroscopy and optical rotary dispersion of zein, wheat gluten and gliadin J Phys Chem 61 1627 1631 10.1021/j150558a014 1:CAS:528:DyaG1cXivVKitA%3D%3D
    • (1957) J Phys Chem , vol.61 , pp. 1627-1631
    • Kretschmer, C.B.1
  • 15
    • 0032524420 scopus 로고    scopus 로고
    • Protein structure in KBr pellets by infrared spectroscopy
    • DOI 10.1006/abio.1998.2599
    • LA Forato R Bernardes-Filho LA Colnago 1998 Protein structure in KBr pellets by infrared spectroscopy Anal Biochem 259 136 141 10.1006/abio.1998.2599 1:CAS:528:DyaK1cXjsFWns7k%3D (Pubitemid 28247061)
    • (1998) Analytical Biochemistry , vol.259 , Issue.1 , pp. 136-141
    • Forato, L.A.1    Bernardes-Filho, R.2    Colnago, L.A.3
  • 16
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • 1:CAS:528:DyaK2MXmvVWlu7s%3D
    • E Goormaghtigh V Cabiaux J-M Ruysschaert 1994 Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures Subcell Biochem 23 405 450 1:CAS:528:DyaK2MXmvVWlu7s%3D
    • (1994) Subcell Biochem , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 18
    • 0023377695 scopus 로고
    • Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region
    • 10.1016/S0006-3495(87)83189-2 1:CAS:528:DyaL2sXlsV2mtL8%3D
    • G Anderle R Mendelsohn 1987 Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region Biophys J 52 69 74 10.1016/S0006-3495(87)83189-2 1:CAS:528:DyaL2sXlsV2mtL8%3D
    • (1987) Biophys J , vol.52 , pp. 69-74
    • Anderle, G.1    Mendelsohn, R.2
  • 19
    • 0023288712 scopus 로고
    • Study of the amide III band by FT-IR spectrometry of the secondary structure of albumin, myoglobin, and gamma -globulin
    • K Kaiden T Matsui S Tanaka 1987 Study of the amide III band by FTIR spectrometry of the secondary structure of albumin, myoglobin, and gamma-globulin Appl Spectrosc 41 180 184 10.1366/000370287774986714 1:CAS:528:DyaL2sXktVars7w%3D (Pubitemid 17526874)
    • (1987) Applied Spectroscopy , vol.41 , Issue.2 , pp. 180-184
    • Koichi, K.1    Tomoko, M.2    Shigeyuki, T.3
  • 20
    • 0033584169 scopus 로고    scopus 로고
    • Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins
    • DOI 10.1016/S0301-4622(99)00060-5, PII S0301462299000605
    • S Cai BR Singh 1999 Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins Biophys Chem 80 7 20 10.1016/S0301-4622(99)00060-5 1:CAS:528:DyaK1MXltlKjsb0%3D (Pubitemid 29333160)
    • (1999) Biophysical Chemistry , vol.80 , Issue.1 , pp. 7-20
    • Cai, S.1    Singh, B.R.2
  • 21
    • 34250810231 scopus 로고    scopus 로고
    • Effect of solvent and temperature on secondary and tertiary structure of zein by circular dichroism
    • DOI 10.1094/CCHEM-84-3-0265
    • GW Selling SAH Hamaker DJ Sessa 2007 Effect of solvent and temperature on secondary and tertiary structure of zein by circular dichroism Cereal Chem 84 27 265 10.1094/CCHEM-84-3-0265 (Pubitemid 46981602)
    • (2007) Cereal Chemistry , vol.84 , Issue.3 , pp. 265-270
    • Selling, G.W.1    Hamaker, S.A.H.2    Sessa, D.J.3
  • 22
    • 52449135457 scopus 로고    scopus 로고
    • The effect of sulfhydryl groups and disulphide linkage in the thermal aggregation of Z19 α-zein
    • 10.1016/j.bbapap.2008.04.002 1:CAS:528:DC%2BD1cXnt1Citbw%3D
    • V Cabra E Vazquez-Contreres A Moreno R Arrequin-Espinosa 2008 The effect of sulfhydryl groups and disulphide linkage in the thermal aggregation of Z19 α-zein Biochim Biophys Acta Proteins Proteomics 1784 1028 1036 10.1016/j.bbapap.2008.04.002 1:CAS:528:DC%2BD1cXnt1Citbw%3D
    • (2008) Biochim Biophys Acta Proteins Proteomics , vol.1784 , pp. 1028-1036
    • Cabra, V.1    Vazquez-Contreres, E.2    Moreno, A.3    Arrequin-Espinosa, R.4
  • 24
    • 1642546383 scopus 로고    scopus 로고
    • Computation and Analysis of Protein Circular Dichroism Spectra
    • DOI 10.1016/S0076-6879(04)83013-1
    • N Sreerama RW Woody 2004 Computation and analysis of protein circular dichroism spectra Meth Enzymol 383 318 351 10.1016/S0076-6879(04)83013-1 1:CAS:528:DC%2BD2cXkt1Siu7o%3D (Pubitemid 38401795)
    • (2004) Methods in Enzymology , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.