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Volumn 19, Issue , 2013, Pages 146-152

Cold plasma effects on enzyme activity in a model food system

Author keywords

Cold plasma; Non thermal process; Peroxidase; Polyphenoloxidase; Secondary structure; Tryptophan fluorescence

Indexed keywords

COLD PLASMAS; NON-THERMAL PROCESS; PEROXIDASE; POLYPHENOL OXIDASE; SECONDARY STRUCTURES; TRYPTOPHAN FLUORESCENCE;

EID: 84880052102     PISSN: 14668564     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ifset.2013.04.002     Document Type: Article
Times cited : (278)

References (52)
  • 1
    • 0037880763 scopus 로고
    • Inactivation of mushroom tyrosinase by hydrogen peroxide
    • A. Andrawis, and V. Kahn Inactivation of mushroom tyrosinase by hydrogen peroxide Phytochemistry 24 3 1985 397 405
    • (1985) Phytochemistry , vol.24 , Issue.3 , pp. 397-405
    • Andrawis, A.1    Kahn, V.2
  • 3
    • 0009446662 scopus 로고    scopus 로고
    • 5th ed. Springer-Verlag Berlin, Germany 3-540-66525-0
    • W. Baltes Lebensmittelchemie 5th ed. 2000 Springer-Verlag Berlin, Germany 3-540-66525-0
    • (2000) Lebensmittelchemie
    • Baltes, W.1
  • 5
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • B.S. Berlett, and E.R. Stadtman Protein oxidation in aging, disease, and oxidative stress The Journal of Biological Chemistry 272 33 1997 20313 20316
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 8
    • 68949170818 scopus 로고    scopus 로고
    • Inactivation kinetics of apple polyphenol oxidase in different pressure-temperature domains
    • R. Buckow, U. Weiss, and D. Knorr Inactivation kinetics of apple polyphenol oxidase in different pressure-temperature domains Innovative Food Science and Emerging Technologies 10 2009 441 448
    • (2009) Innovative Food Science and Emerging Technologies , vol.10 , pp. 441-448
    • Buckow, R.1    Weiss, U.2    Knorr, D.3
  • 9
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • E.A. Burstein, N.S. Vedenkina, and M.N. Ivkova Fluorescence and the location of tryptophan residues in protein molecules Photochemistry and Photobiology 18 4 1973 263 279
    • (1973) Photochemistry and Photobiology , vol.18 , Issue.4 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 11
    • 84989726450 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids. III. Cystine and its derivates
    • D. Creed The photophysics and photochemistry of the near-UV absorbing amino acids. III. Cystine and its derivates Photochemistry and Photobiology 39 1984 577 583
    • (1984) Photochemistry and Photobiology , vol.39 , pp. 577-583
    • Creed, D.1
  • 12
    • 0028796185 scopus 로고
    • PH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes
    • T.K. Das, and S. Mazumdar pH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes European Journal of Biochemistry 227 1995 823 828
    • (1995) European Journal of Biochemistry , vol.227 , pp. 823-828
    • Das, T.K.1    Mazumdar, S.2
  • 13
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure
    • A. Davies, and M.E. Delsignore Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure The Journal of Biological Chemistry 262 1987 9908 9913
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 9908-9913
    • Davies, A.1    Delsignore, M.E.2
  • 14
  • 15
    • 10044279737 scopus 로고    scopus 로고
    • Color of minimally processed fruits and vegetables as affected by some chemical and biochemical changes
    • M.S. Tapia, A. Lopez-Malo, S. Alzamora, Springer US 978-0834216723
    • L. Dorantes-Alvarez, and A. Chiralt Color of minimally processed fruits and vegetables as affected by some chemical and biochemical changes M.S. Tapia, A. Lopez-Malo, S. Alzamora, Minimally processed fruits and vegetables: Fundamental aspects and applications 2000 Springer US 978-0834216723 111 126
    • (2000) Minimally Processed Fruits and Vegetables: Fundamental Aspects and Applications , pp. 111-126
    • Dorantes-Alvarez, L.1    Chiralt, A.2
  • 17
    • 84857449518 scopus 로고    scopus 로고
    • Atmospheric pressure plasma treatment of Listeria innocua and Escherichia coli at polysaccharide gel surfaces: Inactivation kinetics and flow cytrometric characterization
    • A. Fröhling, M. Baier, J. Ehlbeck, D. Knorr, and O. Schlüter Atmospheric pressure plasma treatment of Listeria innocua and Escherichia coli at polysaccharide gel surfaces: Inactivation kinetics and flow cytrometric characterization Innovative Food Science and Emerging Technologies 13 2012 142 150
    • (2012) Innovative Food Science and Emerging Technologies , vol.13 , pp. 142-150
    • Fröhling, A.1    Baier, M.2    Ehlbeck, J.3    Knorr, D.4    Schlüter, O.5
  • 18
    • 0020157737 scopus 로고
    • Fluorescence characteristics of kynurenine and N′-formylkynurenine. Their use as reporters of the environment of tryptophan 62 in hen egg-white lysozyme
    • Y. Fukunaga, Y. Katsuragi, T. Izumi, and F. Sakiyama Fluorescence characteristics of kynurenine and N′-formylkynurenine. Their use as reporters of the environment of tryptophan 62 in hen egg-white lysozyme Biochemical Journal 92 1982 129 141
    • (1982) Biochemical Journal , vol.92 , pp. 129-141
    • Fukunaga, Y.1    Katsuragi, Y.2    Izumi, T.3    Sakiyama, F.4
  • 19
    • 0029028452 scopus 로고
    • Early destruction of tryptophan residues of apolipoprotein B is a vitamin E-independent process during copper-mediated oxidation of LDL
    • A. Gießauf, E. Steiner, and H. Esterbauer Early destruction of tryptophan residues of apolipoprotein B is a vitamin E-independent process during copper-mediated oxidation of LDL Biochimica et Biophysica Acta 1256 1995 221 232
    • (1995) Biochimica et Biophysica Acta , vol.1256 , pp. 221-232
    • Gießauf, A.1    Steiner, E.2    Esterbauer, H.3
  • 22
    • 0000427167 scopus 로고
    • Effect of ascorbic acid, sodium bisulfite, and thiol compounds on mushroom polyphenoloxidase
    • A. Golan-Goldhirsch, and J.R. Whitaker Effect of ascorbic acid, sodium bisulfite, and thiol compounds on mushroom polyphenoloxidase Journal of Agricultural and Food Chemistry 32 1984 1003 1009
    • (1984) Journal of Agricultural and Food Chemistry , vol.32 , pp. 1003-1009
    • Golan-Goldhirsch, A.1    Whitaker, J.R.2
  • 23
    • 0021344070 scopus 로고
    • Photochemistry of proteins: A review
    • L.I. Grossweiner Photochemistry of proteins: A review Current Eye Research 3 1984 137 144
    • (1984) Current Eye Research , vol.3 , pp. 137-144
    • Grossweiner, L.I.1
  • 27
    • 0030784326 scopus 로고    scopus 로고
    • Effects of high field electric pulses on the activity of selected enzymes
    • S.Y. Ho, G.S. Mittal, and J.D. Cross Effects of high field electric pulses on the activity of selected enzymes Journal of Food Engineering 31 1997 69 84
    • (1997) Journal of Food Engineering , vol.31 , pp. 69-84
    • Ho, S.Y.1    Mittal, G.S.2    Cross, J.D.3
  • 29
    • 0032071214 scopus 로고    scopus 로고
    • Impact of high intensity electric field pulses on plant membrane permeabilization
    • D. Knorr, and A. Angersbach Impact of high intensity electric field pulses on plant membrane permeabilization Trends in Food Science and Technology 9 1998 185 191
    • (1998) Trends in Food Science and Technology , vol.9 , pp. 185-191
    • Knorr, D.1    Angersbach, A.2
  • 30
    • 40549089488 scopus 로고    scopus 로고
    • Quenching of fluorescence
    • Springer Germany 978-0-387-31278-1
    • J.R. Lakowicz Quenching of fluorescence Principles of fluorescence spectroscopy 2006 Springer Germany 978-0-387-31278-1 278 327
    • (2006) Principles of Fluorescence Spectroscopy , pp. 278-327
    • Lakowicz, J.R.1
  • 31
    • 2142714435 scopus 로고    scopus 로고
    • Evaluation of the roles of reactive species, heat, and UV radiation in the inactivation of bacterial cells by air plasmas at atmospheric pressure
    • M. Laroussi, and F. Leipold Evaluation of the roles of reactive species, heat, and UV radiation in the inactivation of bacterial cells by air plasmas at atmospheric pressure International Journal of Mass Spectrometry 233 1-3 2004 81 86
    • (2004) International Journal of Mass Spectrometry , vol.233 , Issue.13 , pp. 81-86
    • Laroussi, M.1    Leipold, F.2
  • 33
    • 0000582157 scopus 로고
    • Developments of non-thermal processes for food preservation
    • B. Mertens, and D. Knorr Developments of non-thermal processes for food preservation Food Technology 46 1992 124 133
    • (1992) Food Technology , vol.46 , pp. 124-133
    • Mertens, B.1    Knorr, D.2
  • 34
    • 84986870073 scopus 로고
    • Reduction of cresolase and catecholase activities in tubers of some Indian potato varieties by the application of potash fertilisers
    • J.B. Misra, N.P. Sukumaran, and S.C. Verma Reduction of cresolase and catecholase activities in tubers of some Indian potato varieties by the application of potash fertilisers Journal of the Science of Food and Agriculture 54 1991 339 345
    • (1991) Journal of the Science of Food and Agriculture , vol.54 , pp. 339-345
    • Misra, J.B.1    Sukumaran, N.P.2    Verma, S.C.3
  • 35
    • 0006750234 scopus 로고
    • Studies on taka-amylase A under high pressure treatment. II. Recovery of enzymatic activity of pressure inactivated taka-amylase A and its enhancement by retreatment at moderate pressure
    • K. Miyagawa, K. Sannoe, and K. Suzuki Studies on taka-amylase A under high pressure treatment. II. Recovery of enzymatic activity of pressure inactivated taka-amylase A and its enhancement by retreatment at moderate pressure Archives of Biochemistry and Biophysics 106 1964 467 474
    • (1964) Archives of Biochemistry and Biophysics , vol.106 , pp. 467-474
    • Miyagawa, K.1    Sannoe, K.2    Suzuki, K.3
  • 37
    • 0014409091 scopus 로고
    • Conformation of cytochromes. II. Comparative study of circular dichroism spectra, optical rotatory dispersion, and absorption spectra of horse heart cytochrome
    • Y.P. Myer Conformation of cytochromes. II. Comparative study of circular dichroism spectra, optical rotatory dispersion, and absorption spectra of horse heart cytochrome Biological Chemistry 243 1968 2115 2122
    • (1968) Biological Chemistry , vol.243 , pp. 2115-2122
    • Myer, Y.P.1
  • 38
    • 0025237349 scopus 로고
    • Protein damage induced by small amounts of photodynamically generated singlet oxygen or hydroxyl radicals
    • C. Prinsze, T.M.A.R. Dubbleman, and J.V. Steveninck Protein damage induced by small amounts of photodynamically generated singlet oxygen or hydroxyl radicals Biochimica et Biophysica Acta 1038 1990 152 157
    • (1990) Biochimica et Biophysica Acta , vol.1038 , pp. 152-157
    • Prinsze, C.1    Dubbleman, T.M.A.R.2    Steveninck, J.V.3
  • 43
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • E.R. Stadtman, and R.L. Levine Free radical-mediated oxidation of free amino acids and amino acid residues in proteins Amino Acids 25 2003 207 218
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 45
    • 0002185157 scopus 로고
    • Sulfites as food ingredients
    • S.L. Taylor, and R.K. Bush Sulfites as food ingredients Food Technology 40 1986 47 52
    • (1986) Food Technology , vol.40 , pp. 47-52
    • Taylor, S.L.1    Bush, R.K.2
  • 47
    • 0003349223 scopus 로고
    • Prevention of enzymatic browning in fruits and vegetables. A review of Principles and practice
    • C.Y. Lee, J.R. Whitaker, American Chemical Society Washington, DC
    • L. Vámos-Vigyázó Prevention of enzymatic browning in fruits and vegetables. A review of Principles and practice C.Y. Lee, J.R. Whitaker, Enzymatic browning and its prevention 1995 American Chemical Society Washington, DC 49 62
    • (1995) Enzymatic Browning and Its Prevention , pp. 49-62
    • Vámos-Vigyázó, L.1
  • 48
    • 1542377346 scopus 로고    scopus 로고
    • Protein-lipid interactions during liposome oxidation with added anthocyanin and other phenolic compounds
    • K. Viljanen, R. Kivikari, and M. Heinonen Protein-lipid interactions during liposome oxidation with added anthocyanin and other phenolic compounds Journal of Agricultural and Food Chemistry 52 2004 1104 1111
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 1104-1111
    • Viljanen, K.1    Kivikari, R.2    Heinonen, M.3
  • 49
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • J.T. Vivian, and P.R. Callis Mechanisms of tryptophan fluorescence shifts in proteins Biophysical Journal 80 2001 2093 2109
    • (2001) Biophysical Journal , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 52
    • 33745186912 scopus 로고    scopus 로고
    • Inactivation kinetics and secondary structural change of PEF-treated POD and PPO
    • K. Zhong, J. Wu, Z. Wang, F. Chen, X. Liao, and X. Hu Inactivation kinetics and secondary structural change of PEF-treated POD and PPO Food Chemistry 100 2007 115 123
    • (2007) Food Chemistry , vol.100 , pp. 115-123
    • Zhong, K.1    Wu, J.2    Wang, Z.3    Chen, F.4    Liao, X.5    Hu, X.6


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