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Volumn 6, Issue 1, 2002, Pages 65-76

Effect of temperature, ph, ionic strength, and sodium nitrate on activity of lips: Implications for bioremediation

Author keywords

[No Author keywords available]

Indexed keywords

EFFECT OF TEMPERATURE; ENVIRONMENTAL PARAMETER; ENZYME STABILITY; HIGH ACTIVITY; IMMOBILIZED CULTURE; LITERATURE DATA; OXIDATION REACTIONS; PHANEROCHAETE CHRYSOSPORIUM; SODIUM NITRATES; TEMPERATURE RANGE; TIME DECAY CONSTANT; WASTE BIOREMEDIATION; WORKING CONDITIONS;

EID: 0012957577     PISSN: 10889868     EISSN: 15476529     Source Type: Journal    
DOI: 10.1080/10889860290777486     Document Type: Article
Times cited : (16)

References (26)
  • 1
    • 0027653034 scopus 로고
    • Waste treatment applications of enzymes: opportunities and obstacles
    • Aitken, M.D. 1993. Waste Treatment Applications of Enzymes: Opportunities and Obstacles. Chem. Eng. J. 52:B49-B58. (Pubitemid 276162)
    • (1993) Chemical Engineering Journal , vol.52 , Issue.2
    • Aitken, M.D.1
  • 2
    • 0024962636 scopus 로고
    • Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium
    • Aitken, M.D. and R.L. Irvine. 1989. Stability Testing of Ligninase and Mn-Peroxidase from Phanerochaete chrysosporium. Biotechnol. Bioeng. 34:1251-1260. (Pubitemid 20051897)
    • (1989) Biotechnology and Bioengineering , vol.34 , Issue.10 , pp. 1251-1260
    • Aitken, M.D.1    Irvine, R.L.2
  • 3
    • 0028501805 scopus 로고
    • Characterization of reaction products from the enzyme catalyzed oxidation of phenolic pollutants
    • Aitken, M.D., I.J. Massey, T. Chen, and P.E. Heck. 1994. Characterization of Reaction Products from the Enzyme Catalyzed Oxidation of Phenolic Pollutants. Water Res. 28(9):1879-1889 .
    • (1994) Water Res. , vol.28 , Issue.9 , pp. 1879-1889
    • Aitken, M.D.1    Massey, I.J.2    Chen, T.3    Heck, P.E.4
  • 4
    • 0023661643 scopus 로고
    • Lignin peroxidase: Resonance raman spectral evidence for compound ii and for a temperaturedependent coordination-state equilibrium in the ferric enzyme
    • Andersson, L.A., V. Renganathan, T.M. Loehr, and M.H. Gold. 1987. Lignin Peroxidase: Resonance Raman Spectral Evidence for Compound II and for a Temperaturedependent Coordination-state Equilibrium in the Ferric Enzyme. Biochemistry. 26:2258-2263.
    • (1987) Biochemistry. , vol.26 , pp. 2258-2263
    • Andersson, L.A.1    Renganathan, V.2    Loehr, T.M.3    Gold, M.H.4
  • 5
    • 0342813156 scopus 로고    scopus 로고
    • Structural properties of peroxidases
    • DOI 10.1016/S0168-1656(97)01677-5, PII S0168165697016775
    • Banci, L. 1997. Structural Properties of Peroxidases. J. Biotechnol. 53:253-263. (Pubitemid 27286441)
    • (1997) Journal of Biotechnology , vol.53 , Issue.2-3 , pp. 253-263
    • Banci, L.1
  • 6
    • 0026616392 scopus 로고
    • Decontaminating soil with enzymes
    • Bollag, J.M. 1992. Decontaminating Soil with Enzymes. Environ. Sci. Technol. 26(10):1876-1881.
    • (1992) Environ. Sci. Technol. , vol.26 , Issue.10 , pp. 1876-1881
    • Bollag, J.M.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M. (1976). A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein Dye Binding. Anal. Biochem., 72:248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0008892656 scopus 로고    scopus 로고
    • Optimization of cultural conditions for production of lignin peroxidases by Phanerochaete chrysosporium
    • Bosco, F., B. Ruggeri, and G. Sassi. 1999. Optimization of Cultural Conditions for Production of Lignin Peroxidases by Phanerochaete chrysosporium. Microbios. 98:35-49. (Pubitemid 129637614)
    • (1999) Microbios , vol.98 , Issue.389 , pp. 35-49
    • Bosco, F.1    Ruggeri, B.2    Sassi, G.3
  • 9
    • 84982512382 scopus 로고
    • Biodegradation of environmental pollutants by the white rot fungus phanerochaete chrysosporium: Involvement of the lignin degrading system
    • Bumpus, J.A., and S.D. Aust. 1987. Biodegradation of Environmental Pollutants by the White Rot Fungus Phanerochaete chrysosporium: Involvement of the Lignin Degrading System. Bioessays 6(4):166-170.
    • (1987) Bioessays , vol.6 , Issue.4 , pp. 166-170
    • Bumpus, J.A.1    Aust, S.D.2
  • 10
    • 0026350736 scopus 로고
    • Lignin peroxidase of phanerochaete chrysosporium
    • Cai, D. and M. Tien. 1991. Lignin Peroxidase of Phanerochaete chrysosporium. J. Biol. Chem. 266(22):14464-14469.
    • (1991) J. Biol. Chem. , vol.266 , Issue.22 , pp. 14464-14469
    • Cai, D.1    Tien, M.2
  • 11
    • 0027279381 scopus 로고
    • Lignin-degrading peroxidases of phanerochaete chrysosporium
    • Cai, D. and M. Tien. 1993. Lignin-degrading Peroxidases of Phanerochaete chrysosporium. J. Biotechnol. 30:79-90.
    • (1993) J. Biotechnol. , vol.30 , pp. 79-90
    • Cai, D.1    Tien, M.2
  • 13
    • 84858268570 scopus 로고
    • Tintostamperia: Depurazione e riutilizzo acque di scarico
    • De Ponti, E. 1993. Tintostamperia: Depurazione e Riutilizzo Acque di Scarico. Tecnologie Tessili. 7(9):74-79.
    • (1993) Tecnologie Tessili. , vol.7 , Issue.9 , pp. 74-79
    • De Ponti, E.1
  • 14
    • 0021101692 scopus 로고
    • An extracellular h2o2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete phanerochaete chrysosporium
    • Glenn, K.J., M.A. Morgan, M.B. Mayfield, M. Kuwahara, and M.H. Gold. 1983. An Extracellular H2O2-requiring Enzyme Preparation Involved in Lignin Biodegradation by the White Rot Basidiomycete Phanerochaete chrysosporium. Biochem. Biophys. Res. Commun. 114:1077-1083.
    • (1983) Biochem. Biophys. Res. Commun. , vol.114 , pp. 1077-1083
    • Glenn, K.J.1    Morgan, M.A.2    Mayfield, M.B.3    Kuwahara, M.4    Gold, M.H.5
  • 15
    • 0004140974 scopus 로고
    • The Application of Enzyme in Industry. The Nature Press, New York
    • Godfrey, T., and T. Reichelt. 1983. Industrial Enzymology. The Application of Enzyme in Industry. The Nature Press, New York.
    • (1983) Industrial Enzymology
    • Godfrey, T.1    Reichelt, T.2
  • 16
    • 0031172251 scopus 로고    scopus 로고
    • Potential applications of enzymes in waste treatment
    • DOI 10.1002/(SICI)1097-4660(199706)69:2<141::AID-JCTB694>3.0.CO;2-U
    • Karam, J. and A. Nicell. 1997. Potential Application of Enzyme in Waste Treatment. J. Chem. Technol. Biotechnol. 69:141-153. (Pubitemid 27257600)
    • (1997) Journal of Chemical Technology and Biotechnology , vol.69 , Issue.2 , pp. 141-153
    • Karam, J.1    Nicell, J.A.2
  • 17
    • 0002736220 scopus 로고    scopus 로고
    • The stability analysis and modeling of pH- and ionic strength inactivation of penicillin G acylase obtained from various species of Escherichia coli
    • PII S1369703X98000217
    • Kheirolomoom, A., M. Ardjmand, M. Vossoughi, and M. Kazemeini. 1998. The Stability Analysis and Modeling of pH-and Ionic Strength Inactivation of Penicillin G Acylase obtained from various Species of Escherichia coli. Biochem. Eng. J. 2:81-88. (Pubitemid 128421132)
    • (1998) Biochemical Engineering Journal , vol.2 , Issue.2 , pp. 81-88
    • Kheirolomoom, A.1    Ardjmand, M.2    Vossoughi, M.3    Kazemeini, M.4
  • 18
    • 0026588636 scopus 로고
    • Phenol removal from aqueous solutions by peroxidase-catalyzed reaction using additives
    • Nakamoto, S., and N. Machida. 1992. Phenol Removal from Aqueous Solutions by Peroxidase-catalyzed Reaction using Additives. Water Res. 26(1):49-54.
    • (1992) Water Res. , vol.26 , Issue.1 , pp. 49-54
    • Nakamoto, S.1    MacHida, N.2
  • 19
    • 0031568238 scopus 로고    scopus 로고
    • Effect of calcium on the reversible thermal inactivation of lignin peroxidase
    • DOI 10.1006/abbi.1996.9770
    • Nie, G., and S.D. Aust. 1997. Effect of Calcium on the Reversible Thermal Inactivation of Lignin Peroxidase. Arch. Biochem. Biophys. 337(2):225-231. (Pubitemid 27198186)
    • (1997) Archives of Biochemistry and Biophysics , vol.337 , Issue.2 , pp. 225-231
    • Nie, G.1    Aust, S.D.2
  • 20
    • 0027375222 scopus 로고
    • Decolorization of azo, triphenyl methane, heterocyclic, and polymeric dyes by lignin peroxidase isoenzymes from Phanerochaete chrysosporium
    • Ollikka, P., K. Alhonmaki, V.M. Leppanen, T. Glumoff, T. Rajiola, and I. Suominen. 1993. Decolorization of Azo, Triphenyl Methane, Heterocyclic and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium. Appl. Environ. Microbiol. 59:4010-4016. (Pubitemid 23361381)
    • (1993) Applied and Environmental Microbiology , vol.59 , Issue.12 , pp. 4010-4016
    • Ollikka, P.1    Alhonmaki, K.2    Leppanen, V.-M.3    Glumoff, T.4    Raijola, T.5    Suominen, I.6
  • 22
    • 0000230699 scopus 로고
    • Lignin-degrading enzyme from phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique h2o2-requiring oxygenase
    • Tien, M., and T.K. Kirk. 1984. Lignin-degrading Enzyme from Phanerochaete chrysosporium: Purification, Characterization, and Catalytic Properties of a Unique H2O2-requiring Oxygenase. Proc. Natl. Acad. Sci. U.S.A. 81:2280-2284.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2280-2284
    • Tien, M.1    Kirk, T.K.2
  • 23
    • 69749084914 scopus 로고
    • Lignin peroxidase of phanerochaete chrysosporium
    • Tien, M., and T.K. Kirk. 1988. Lignin Peroxidase of Phanerochaete chrysosporium. Methods Enzymol. 23:238-249.
    • (1988) Methods Enzymol. , vol.23 , pp. 238-249
    • Tien, M.1    Kirk, T.K.2
  • 24
    • 0025343321 scopus 로고
    • Lignin peroxidase H2 from Phanerochaete chrysosporium: Purification, characterization and stability to temperature and pH
    • DOI 10.1016/0003-9861(90)90476-F
    • Tuisel, H., R. Sinclair, J.A. Bumpus, W. Ashbaugh, B.J. Brock, and S.D. Aust. 1990. Lignin Peroxidase H2 from Phanerochaete chrysosporium: Purification, Characterization and Stability to Temperature and pH. Arch. Biochem. Biophys. 279:158-166. (Pubitemid 20149787)
    • (1990) Archives of Biochemistry and Biophysics , vol.279 , Issue.1 , pp. 158-166
    • Tuisel, H.1    Sinclair, R.2    Bumpus, J.A.3    Ashbaugh, W.4    Brock, B.J.5    Aust, S.D.6
  • 25
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder, K.G. 1992. Superfamily of Plant, Fungal and Bacterial Peroxidases. Curr. Opin. Struct. Biol. 2:388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 26
    • 0032889823 scopus 로고    scopus 로고
    • Development of bioreactor systems for decolorization of Orange II using white rot fungus
    • DOI 10.1016/S0141-0229(98)00090-8, PII S0141022998000908
    • Zhang, F., J.S. Knapp, and K.N. Tapley. 1999. Development of Bioreactor Systems for Decolorization of Orange II using White Rot Fungus. Enzyme Microbiol. Technol. 24:48-53. (Pubitemid 28529468)
    • (1999) Enzyme and Microbial Technology , vol.24 , Issue.1-2 , pp. 48-53
    • Zhang, F.-M.1    Knapp, J.S.2    Tapley, K.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.