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Volumn 19, Issue 1, 1996, Pages 50-56

A biosensor stabilized by polyethylene glycol for the monitoring of hydrogen peroxide in organic solvent media

Author keywords

Biosensor; Catalase; Enzyme stabilization; Hydrogen peroxide; Organic solvent; Polyethylene glycol; Polyvinyl alcohol membrane

Indexed keywords

ENZYME KINETICS; ENZYMES; HYDROGEN PEROXIDE; INFRARED SPECTROPHOTOMETERS; MIXING; MOLECULAR WEIGHT; ORGANIC SOLVENTS; POLYETHYLENE GLYCOLS; STABILIZATION;

EID: 0030200283     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/0141-0229(95)00178-6     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0343746263 scopus 로고
    • Peroxides
    • (Mark, H. F., Othmer, D. O., Overberger, C. G., and Seaborg, G. T., Eds.). John Wiley & Sons
    • Kirchner, J. R. Peroxides. In: Kirk-Othmer Encyclopedia of Chemical Technology, Vol. 13 (Mark, H. F., Othmer, D. O., Overberger, C. G., and Seaborg, G. T., Eds.). John Wiley & Sons, 1987, 12-28
    • (1987) Kirk-Othmer Encyclopedia of Chemical Technology , vol.13 , pp. 12-28
    • Kirchner, J.R.1
  • 2
    • 0025651816 scopus 로고
    • Goat liver catalase immobilized on various solid supports
    • Chatterjee, U., Kumer, A., and Sanwal, G. G. Goat liver catalase immobilized on various solid supports. J. Ferment. Bioeng. 1990, 70, 429-430
    • (1990) J. Ferment. Bioeng. , vol.70 , pp. 429-430
    • Chatterjee, U.1    Kumer, A.2    Sanwal, G.G.3
  • 3
    • 0000856583 scopus 로고
    • Spectrophotometric determination of hydrogen peroxide after extraction with ethyl acetate
    • Clapp, P. A., Evans, D. F., and Sheriff, T. P. Spectrophotometric determination of hydrogen peroxide after extraction with ethyl acetate. Anal. Chim. Acta. 1989, 218, 331-334
    • (1989) Anal. Chim. Acta. , vol.218 , pp. 331-334
    • Clapp, P.A.1    Evans, D.F.2    Sheriff, T.P.3
  • 4
    • 37049090807 scopus 로고
    • Improved determination of hydrogen peroxide or lucigenin by measurement of lucigenin chemiluminescence in organized assemblies
    • Malehorn, C. L., Hinze, W. L., and Riehl, T. E. Improved determination of hydrogen peroxide or lucigenin by measurement of lucigenin chemiluminescence in organized assemblies. Analyst 1986, 111, 941-947
    • (1986) Analyst , vol.111 , pp. 941-947
    • Malehorn, C.L.1    Hinze, W.L.2    Riehl, T.E.3
  • 7
    • 0005312139 scopus 로고
    • A specific bioelectrochemical sensor for hydrogen peroxide
    • Aizawa, M., Karube, I., and Suzuki, S. A specific bioelectrochemical sensor for hydrogen peroxide. Anal. Chim. Acta. 1974, 69, 431-437
    • (1974) Anal. Chim. Acta. , vol.69 , pp. 431-437
    • Aizawa, M.1    Karube, I.2    Suzuki, S.3
  • 8
    • 0024998047 scopus 로고
    • Biosensor for determination of hydrogen peroxide based on catalase activity of human erythrocytes
    • Racek, J., and Peter, R. Biosensor for determination of hydrogen peroxide based on catalase activity of human erythrocytes. Anal. Chim. Acta. 1990, 239, 19-22
    • (1990) Anal. Chim. Acta. , vol.239 , pp. 19-22
    • Racek, J.1    Peter, R.2
  • 10
    • 0022806012 scopus 로고
    • The developing biosensor arena
    • Hall, W. A. H. The developing biosensor arena. Enzyme Microb. Technol. 1986, 8, 651-658
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 651-658
    • Hall, W.A.H.1
  • 11
    • 0343310531 scopus 로고
    • Biosensor for the monitoring of hydrogen peroxide using poly(vinyl alcohol) membrane system
    • Joo, H., and Yoo, Y. J. Biosensor for the monitoring of hydrogen peroxide using poly(vinyl alcohol) membrane system. Biotechnol. Tech. 1991, 5, 453-458
    • (1991) Biotechnol. Tech. , vol.5 , pp. 453-458
    • Joo, H.1    Yoo, Y.J.2
  • 12
    • 0000321692 scopus 로고
    • Enzyme-catalyzed processes in organic solvents
    • Zaks, A., and Klibanov, A. M. Enzyme-catalyzed processes in organic solvents. Proc. Natl. Acad. Sci. 1985, 82, 3192-3196
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 3192-3196
    • Zaks, A.1    Klibanov, A.M.2
  • 13
    • 0026136572 scopus 로고
    • Effect of a water-miscible organic solvent on the kinetic and structural properties of trypsin
    • Guinn, R. M., Blanch, H. W., and Clark, D. S. Effect of a water-miscible organic solvent on the kinetic and structural properties of trypsin. Enzyme Microb. Technol. 1991, 13, 320-326
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 320-326
    • Guinn, R.M.1    Blanch, H.W.2    Clark, D.S.3
  • 14
    • 0028472579 scopus 로고
    • Storage stabilization and purification of enzyme by water-soluble synthetic polymers
    • Bryjak, J., and Noworyta, A. Storage stabilization and purification of enzyme by water-soluble synthetic polymers. Enzyme Microb. Technol. 1994, 16, 616-621
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 616-621
    • Bryjak, J.1    Noworyta, A.2
  • 15
    • 0343310529 scopus 로고
    • The activity of PEG-modified chymotrypsin in aqueous and organic media
    • Pina, C., Clark, D., and Blanch, H. The activity of PEG-modified chymotrypsin in aqueous and organic media. Biotechnol. Tech. 1990, 5, 333-338
    • (1990) Biotechnol. Tech. , vol.5 , pp. 333-338
    • Pina, C.1    Clark, D.2    Blanch, H.3
  • 16
    • 0006496573 scopus 로고
    • Complexation between poly(dimethyl-diallyl-ammonium chloride) and globular proteins
    • (Hamel, J. P. F., Hunter, J. B., and Sikdar, S. K., eds.). American Chemical Society. Washington, D.C.
    • Strege, M. A., Dubin, P. L., West, J. S., and Flinta, C. D. Complexation between poly(dimethyl-diallyl-ammonium chloride) and globular proteins. In: Downstream Processing and Bioseparation (Hamel, J. P. F., Hunter, J. B., and Sikdar, S. K., eds.). American Chemical Society. Washington, D.C., 1990, 158-169
    • (1990) Downstream Processing and Bioseparation , pp. 158-169
    • Strege, M.A.1    Dubin, P.L.2    West, J.S.3    Flinta, C.D.4
  • 17
    • 0343310528 scopus 로고
    • Pervaporation of water-ethanol with PVA-fluoropore composite membrane
    • (Bakish, R., Eds.). Bakish Material Corporation, Englewood, N.J.
    • Yamada, S., Nakagawa, T., and Abo, T. Pervaporation of water-ethanol with PVA-fluoropore composite membrane. In: Proc. Fourth Int. Conf. Pervaporation Proc. Chem. Ind. (Bakish, R., Eds.). Bakish Material Corporation, Englewood, N.J. 1989, 64-74
    • (1989) Proc. Fourth Int. Conf. Pervaporation Proc. Chem. Ind. , pp. 64-74
    • Yamada, S.1    Nakagawa, T.2    Abo, T.3
  • 18
    • 77957006400 scopus 로고
    • Assay of catalase and peroxidases
    • (Colowick, S. P., and Kaplan, N. O., Eds.). Academic Press, New York
    • Chance, B., and Maehly, A. C. Assay of catalase and peroxidases. In: Methods in Enzymology Vol. 2, (Colowick, S. P., and Kaplan, N. O., Eds.). Academic Press, New York, 1963, 764-775
    • (1963) Methods in Enzymology , vol.2 , pp. 764-775
    • Chance, B.1    Maehly, A.C.2
  • 19
    • 0025101108 scopus 로고
    • Ultrafiltration membranes as carriers for lipase immobilization
    • Rucka, M., and Turkiewicz, B. Ultrafiltration membranes as carriers for lipase immobilization. Enzyme Microb. Technol. 1990, 12, 52-55
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 52-55
    • Rucka, M.1    Turkiewicz, B.2
  • 20
    • 11744301314 scopus 로고
    • Membrane technology
    • (Mark, H. F., Othmer, D. O., Overberger, C. G., and Seaborg, G. T., Eds.). John Wiley & Sons
    • Paul, D. R., and Morel, G. Membrane technology. In: Kirk-Othmer Encyclopedia of Chemical Technology Vol. 15 (Mark, H. F., Othmer, D. O., Overberger, C. G., and Seaborg, G. T., Eds.). John Wiley & Sons, 1987, 92-131
    • (1987) Kirk-Othmer Encyclopedia of Chemical Technology , vol.15 , pp. 92-131
    • Paul, D.R.1    Morel, G.2
  • 21
    • 0015131240 scopus 로고
    • Studies on bovine pancreatic ribonuclease A and compounds in aqueous 2-methyl-2,4-pentanediol
    • Pittz, E. P., and Bello, J. Studies on bovine pancreatic ribonuclease A and compounds in aqueous 2-methyl-2,4-pentanediol. Arch. Biochem. Biophys. 1971, 146, 513-524
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 513-524
    • Pittz, E.P.1    Bello, J.2
  • 22
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki, A., and King, J. Protein folding intermediates and inclusion body formation. Biotechnology 1989, 7, 690-697
    • (1989) Biotechnology , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 23
    • 76549182497 scopus 로고
    • The structural changes of RNase in aqueous urea, ethylene glycol, and ethanol
    • Nozaki, Y., and Tanford, C. The structural changes of RNase in aqueous urea, ethylene glycol, and ethanol. J. Biol. Biophys. 1965, 240, 3568-3571
    • (1965) J. Biol. Biophys. , vol.240 , pp. 3568-3571
    • Nozaki, Y.1    Tanford, C.2
  • 24
    • 0016993508 scopus 로고
    • Applications of the pervaporation process to separate azeotropic mixtures
    • Aptel, P., Challard, N., Cuny, J., and Neel, J. Applications of the pervaporation process to separate azeotropic mixtures. J. Membrane Sci. 1976, 1, 271-287
    • (1976) J. Membrane Sci. , vol.1 , pp. 271-287
    • Aptel, P.1    Challard, N.2    Cuny, J.3    Neel, J.4
  • 25
    • 0014662299 scopus 로고
    • Optical activity of biopolymers
    • Gratzer, W. B., and Cowburn, D. A. Optical activity of biopolymers. Nature 1969, 222, 426-431
    • (1969) Nature , vol.222 , pp. 426-431
    • Gratzer, W.B.1    Cowburn, D.A.2
  • 30
    • 0000467430 scopus 로고
    • Permeation properties
    • (Allen, G. and Bevington, J. C., Eds.). Pergamon Press, Oxford
    • Naylor, T. Permeation properties. In: Comprehensive Polymer Science Vol. 2 (Allen, G. and Bevington, J. C., Eds.). Pergamon Press, Oxford, 1989, 643-668
    • (1989) Comprehensive Polymer Science , vol.2 , pp. 643-668
    • Naylor, T.1
  • 32
    • 0027703820 scopus 로고
    • Effect of water-miscible organic solvents on the catalytic activity of cytochrome c
    • Vazquez, D. R., Semple, K. M., Westlake, D. W. S., and Fedorak, P. B. Effect of water-miscible organic solvents on the catalytic activity of cytochrome c. Enzyme Microb. Technol. 1993, 15, 936-943
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 936-943
    • Vazquez, D.R.1    Semple, K.M.2    Westlake, D.W.S.3    Fedorak, P.B.4
  • 33
    • 14744269612 scopus 로고
    • Cosolvent assisted protein refolding
    • Cleland, J. L., and Wang, D. I. C. Cosolvent assisted protein refolding. Biotechnology 1990, 8, 1274-1278
    • (1990) Biotechnology , vol.8 , pp. 1274-1278
    • Cleland, J.L.1    Wang, D.I.C.2
  • 34
    • 0024060331 scopus 로고
    • Influence of additives on the thermostability of glucose oxidase
    • Ye, W. N., Combes, D., and Monsan, P. Influence of additives on the thermostability of glucose oxidase. Enzyme Microb. Technol. 1988, 10, 498-502
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 498-502
    • Ye, W.N.1    Combes, D.2    Monsan, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.