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Volumn 58, Issue , 2016, Pages 11-19

Effect of heat treatment on physical, structural, thermal and morphological characteristics of zein in ethanol-water solution

Author keywords

Heat treatment; Morphology; Structure; Thermal behaviors; Zein

Indexed keywords

DIFFERENTIAL SCANNING CALORIMETRY; ETHANOL; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; PROTEINS; THERMODYNAMIC STABILITY;

EID: 84958767587     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.02.014     Document Type: Article
Times cited : (113)

References (42)
  • 2
    • 84928493730 scopus 로고    scopus 로고
    • Effect of thermal treatment on secondary structure and conformational change of mushroom polyphenol oxidase (PPO) as food quality related enzyme: a FTIR study
    • Baltacioğlu H., Bayindirli A., Severcan M., Severcan F. Effect of thermal treatment on secondary structure and conformational change of mushroom polyphenol oxidase (PPO) as food quality related enzyme: a FTIR study. Food Chemistry 2015, 187:263-269.
    • (2015) Food Chemistry , vol.187 , pp. 263-269
    • Baltacioğlu, H.1    Bayindirli, A.2    Severcan, M.3    Severcan, F.4
  • 7
    • 77956057741 scopus 로고    scopus 로고
    • Fluorescence spectroscopic study on the interaction of resveratrol with lipoxygenase
    • del Carmen Pinto M., Duque A.L., Macías P. Fluorescence spectroscopic study on the interaction of resveratrol with lipoxygenase. Journal of Molecular Structure 2010, 980(1):143-148.
    • (2010) Journal of Molecular Structure , vol.980 , Issue.1 , pp. 143-148
    • del Carmen Pinto, M.1    Duque, A.L.2    Macías, P.3
  • 8
    • 84883612687 scopus 로고    scopus 로고
    • Understanding of dispersion and aggregation of suspensions of zein nanoparticles in aqueous alcohol solutions after thermal treatment
    • Chen Y., Ye R., Liu J. Understanding of dispersion and aggregation of suspensions of zein nanoparticles in aqueous alcohol solutions after thermal treatment. Industrial Crops and Products 2013, 50:764-770.
    • (2013) Industrial Crops and Products , vol.50 , pp. 764-770
    • Chen, Y.1    Ye, R.2    Liu, J.3
  • 9
    • 70149119887 scopus 로고    scopus 로고
    • Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate
    • Corredig M. Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate. Food Hydrocolloids 2009, 23(8):2141-2148.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2141-2148
    • Corredig, M.1
  • 10
    • 2342430539 scopus 로고    scopus 로고
    • Basic study of corn protein, zein, as a biomaterial in tissue engineering, surface morphology and biocompatibility
    • Dong J., Sun Q., Wang J.Y. Basic study of corn protein, zein, as a biomaterial in tissue engineering, surface morphology and biocompatibility. Biomaterials 2004, 25(19):4691-4697.
    • (2004) Biomaterials , vol.25 , Issue.19 , pp. 4691-4697
    • Dong, J.1    Sun, Q.2    Wang, J.Y.3
  • 11
    • 68149142319 scopus 로고    scopus 로고
    • Glycation and phosphorylation of α-lactalbumin by dry heating: effect on protein structure and physiological functions
    • Enomoto H., Hayashi Y., Li C.P., Ohki S., Ohtomo H., Shiokawa M., et al. Glycation and phosphorylation of α-lactalbumin by dry heating: effect on protein structure and physiological functions. Journal of Dairy Science 2009, 92(7):3057-3068.
    • (2009) Journal of Dairy Science , vol.92 , Issue.7 , pp. 3057-3068
    • Enomoto, H.1    Hayashi, Y.2    Li, C.P.3    Ohki, S.4    Ohtomo, H.5    Shiokawa, M.6
  • 12
    • 77952461957 scopus 로고    scopus 로고
    • Modified zein and its production
    • JP.
    • Funatsu, G., & Shibata, M. (1998). Modified zein and its production. Patent JP, 10017595.
    • (1998)
    • Funatsu, G.1    Shibata, M.2
  • 14
    • 15744372123 scopus 로고    scopus 로고
    • Nano-structure and properties of maize zein studied by atomic force microscopy
    • Guo Y., Liu Z., An H., Li M., Hu J. Nano-structure and properties of maize zein studied by atomic force microscopy. Journal of Cereal Science 2005, 41(3):277-281.
    • (2005) Journal of Cereal Science , vol.41 , Issue.3 , pp. 277-281
    • Guo, Y.1    Liu, Z.2    An, H.3    Li, M.4    Hu, J.5
  • 15
    • 84878164984 scopus 로고    scopus 로고
    • Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes
    • Haque M.A., Aldred P., Chen J., Barrow C.J., Adhikari B. Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes. Food chemistry 2013, 141(2):702-711.
    • (2013) Food chemistry , vol.141 , Issue.2 , pp. 702-711
    • Haque, M.A.1    Aldred, P.2    Chen, J.3    Barrow, C.J.4    Adhikari, B.5
  • 16
    • 84952975489 scopus 로고    scopus 로고
    • Influence of heating treatment and membrane concentration on the formation of soluble aggregates
    • Li Y., Dalgleish D., Corredig M. Influence of heating treatment and membrane concentration on the formation of soluble aggregates. Food Research International 2015, 76:309-316.
    • (2015) Food Research International , vol.76 , pp. 309-316
    • Li, Y.1    Dalgleish, D.2    Corredig, M.3
  • 17
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A., Whitmore L., Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18(1):211-212.
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 18
    • 79955652517 scopus 로고    scopus 로고
    • Preparation and characterization of zein/chitosan complex for encapsulation of α-tocopherol, and its in vitro controlled release study
    • Luo Y., Zhang B., Whent M., Yu L.L., Wang Q. Preparation and characterization of zein/chitosan complex for encapsulation of α-tocopherol, and its in vitro controlled release study. Colloids and Surfaces B: Biointerfaces 2011, 85(2):145-152.
    • (2011) Colloids and Surfaces B: Biointerfaces , vol.85 , Issue.2 , pp. 145-152
    • Luo, Y.1    Zhang, B.2    Whent, M.3    Yu, L.L.4    Wang, Q.5
  • 20
    • 0000056508 scopus 로고
    • Water-soluble zein by enzymatic modification in organic solvents
    • 115-115
    • Mannheim A., Cheryan M. Water-soluble zein by enzymatic modification in organic solvents. Cereal chemistry 1993, 70. 115-115.
    • (1993) Cereal chemistry , vol.70
    • Mannheim, A.1    Cheryan, M.2
  • 21
    • 35448957157 scopus 로고    scopus 로고
    • Circular dichroism and its application to the study of biomolecules
    • Martin S.R., Schilstra M.J. Circular dichroism and its application to the study of biomolecules. Methods in Cell Biology 2008, 84:263-293.
    • (2008) Methods in Cell Biology , vol.84 , pp. 263-293
    • Martin, S.R.1    Schilstra, M.J.2
  • 24
    • 0036824063 scopus 로고    scopus 로고
    • Thermal aggregation of globulin from an indigenous Chinese legume, Phaseolus angularis (red bean)
    • Meng G.T., Ching K.M., Ma C.Y. Thermal aggregation of globulin from an indigenous Chinese legume, Phaseolus angularis (red bean). Food Chemistry 2002, 79(1):93-103.
    • (2002) Food Chemistry , vol.79 , Issue.1 , pp. 93-103
    • Meng, G.T.1    Ching, K.M.2    Ma, C.Y.3
  • 26
    • 84867058987 scopus 로고    scopus 로고
    • Encapsulation of food grade antioxidant in natural biopolymer by electrospinning technique: a physicochemical study based on zein-gallic acid system
    • Neo Y.P., Ray S., Jin J., Gizdavic-Nikolaidis M., Nieuwoudt M.K., Liu D., et al. Encapsulation of food grade antioxidant in natural biopolymer by electrospinning technique: a physicochemical study based on zein-gallic acid system. Food chemistry 2013, 136(2):1013-1021.
    • (2013) Food chemistry , vol.136 , Issue.2 , pp. 1013-1021
    • Neo, Y.P.1    Ray, S.2    Jin, J.3    Gizdavic-Nikolaidis, M.4    Nieuwoudt, M.K.5    Liu, D.6
  • 27
    • 75149162776 scopus 로고    scopus 로고
    • Effect of heat treatment on milk protein functionality at emulsion interfaces. A review
    • Raikos V. Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocolloids 2010, 24(4):259-265.
    • (2010) Food Hydrocolloids , vol.24 , Issue.4 , pp. 259-265
    • Raikos, V.1
  • 29
    • 34250810231 scopus 로고    scopus 로고
    • Effect of solvent and temperature on secondary and tertiary structure of zein by circular dichroism
    • Selling G.W., Hamaker S.A., Sessa D.J. Effect of solvent and temperature on secondary and tertiary structure of zein by circular dichroism. Cereal Chemistry 2007, 84(3):265-270.
    • (2007) Cereal Chemistry , vol.84 , Issue.3 , pp. 265-270
    • Selling, G.W.1    Hamaker, S.A.2    Sessa, D.J.3
  • 30
    • 84922287108 scopus 로고    scopus 로고
    • Effect of heat treatment on structure and immunogenicity of recombinant peanut protein Ara h 2.01
    • Shen L.L., Zhu Q.Q., Huang F.W., Xu H., Wu X.L., Xiao H.F., et al. Effect of heat treatment on structure and immunogenicity of recombinant peanut protein Ara h 2.01. LWT-Food Science and Technology 2015, 60(2):964-969.
    • (2015) LWT-Food Science and Technology , vol.60 , Issue.2 , pp. 964-969
    • Shen, L.L.1    Zhu, Q.Q.2    Huang, F.W.3    Xu, H.4    Wu, X.L.5    Xiao, H.F.6
  • 31
    • 0034824517 scopus 로고    scopus 로고
    • Zein: the industrial protein from corn
    • Shukla R., Cheryan M. Zein: the industrial protein from corn. Industrial Crops and Products 2001, 13(3):171-192.
    • (2001) Industrial Crops and Products , vol.13 , Issue.3 , pp. 171-192
    • Shukla, R.1    Cheryan, M.2
  • 33
    • 80054921076 scopus 로고    scopus 로고
    • Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin
    • Tong P., Gao J., Chen H., Li X., Zhang Y., Jian S., et al. Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chemistry 2012, 131(2):603-610.
    • (2012) Food Chemistry , vol.131 , Issue.2 , pp. 603-610
    • Tong, P.1    Gao, J.2    Chen, H.3    Li, X.4    Zhang, Y.5    Jian, S.6
  • 34
    • 38849131437 scopus 로고    scopus 로고
    • Characterization of the morphology and thermal properties of zein prolamine nanostructures obtained by electrospinning
    • Torres-Giner S., Gimenez E., Lagarón J.M. Characterization of the morphology and thermal properties of zein prolamine nanostructures obtained by electrospinning. Food Hydrocolloids 2008, 22(4):601-614.
    • (2008) Food Hydrocolloids , vol.22 , Issue.4 , pp. 601-614
    • Torres-Giner, S.1    Gimenez, E.2    Lagarón, J.M.3
  • 35
    • 84908520775 scopus 로고    scopus 로고
    • Determination of heat-induced changes in the protein secondary structure of reconstituted livetins (water-soluble proteins from hen's egg yolk) by FTIR
    • Ulrichs T., Drotleff A.M., Ternes W. Determination of heat-induced changes in the protein secondary structure of reconstituted livetins (water-soluble proteins from hen's egg yolk) by FTIR. Food Chemistry 2015, 172:909-920.
    • (2015) Food Chemistry , vol.172 , pp. 909-920
    • Ulrichs, T.1    Drotleff, A.M.2    Ternes, W.3
  • 36
    • 33746219698 scopus 로고    scopus 로고
    • Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0
    • Unterhaslberger G., Schmitt C., Sanchez C., Appolonia-Nouzille C., Raemy A. Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0. Food Hydrocolloids 2006, 20(7):1006-1019.
    • (2006) Food Hydrocolloids , vol.20 , Issue.7 , pp. 1006-1019
    • Unterhaslberger, G.1    Schmitt, C.2    Sanchez, C.3    Appolonia-Nouzille, C.4    Raemy, A.5
  • 37
    • 33744534909 scopus 로고    scopus 로고
    • Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy
    • Wada R., Fujita Y., Kitabatake N. Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochimica et Biophysica Acta (BBA)-General Subjects 2006, 1760(6):841-847.
    • (2006) Biochimica et Biophysica Acta (BBA)-General Subjects , vol.1760 , Issue.6 , pp. 841-847
    • Wada, R.1    Fujita, Y.2    Kitabatake, N.3
  • 38
    • 84861199701 scopus 로고    scopus 로고
    • Antioxidant and antimicrobial properties of essential oils encapsulated in zein nanoparticles prepared by liquid-liquid dispersion method
    • Wu Y., Luo Y., Wang Q. Antioxidant and antimicrobial properties of essential oils encapsulated in zein nanoparticles prepared by liquid-liquid dispersion method. LWT-Food Science and Technology 2012, 48(2):283-290.
    • (2012) LWT-Food Science and Technology , vol.48 , Issue.2 , pp. 283-290
    • Wu, Y.1    Luo, Y.2    Wang, Q.3
  • 40
    • 84875943100 scopus 로고    scopus 로고
    • Probing the binding between norbixin and dairy proteins by spectroscopy methods
    • Zhang Y., Zhong Q. Probing the binding between norbixin and dairy proteins by spectroscopy methods. Food Chemistry 2013, 139(1):611-616.
    • (2013) Food Chemistry , vol.139 , Issue.1 , pp. 611-616
    • Zhang, Y.1    Zhong, Q.2
  • 41
    • 70149102899 scopus 로고    scopus 로고
    • Zein nanoparticles produced by liquid-liquid dispersion
    • Zhong Q., Jin M. Zein nanoparticles produced by liquid-liquid dispersion. Food Hydrocolloids 2009, 23(8):2380-2387.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2380-2387
    • Zhong, Q.1    Jin, M.2
  • 42
    • 64549156880 scopus 로고    scopus 로고
    • Encapsulation of fish oil in solid zein particles by liquid-liquid dispersion
    • Zhong Q., Tian H., Zivanovic S. Encapsulation of fish oil in solid zein particles by liquid-liquid dispersion. Journal of Food Processing and Preservation 2009, 33(2):255-270.
    • (2009) Journal of Food Processing and Preservation , vol.33 , Issue.2 , pp. 255-270
    • Zhong, Q.1    Tian, H.2    Zivanovic, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.