메뉴 건너뛰기




Volumn 178, Issue 1, 2014, Pages 1-11

Versatile peroxidase degradation of humic substances: Use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes

Author keywords

Allosteric regulation; Biphasic sigmoidal Hill's plot; Environmental biotechnology; Enzyme kinetics; Lignin manganese peroxidase

Indexed keywords

CALORIMETERS; CALORIMETRY; DEGRADATION; EFFLUENTS; ENVIRONMENTAL REGULATIONS; ENZYME INHIBITION; ENZYME KINETICS; GROUNDWATER; ISOTHERMS; LIGNIN; MANGANESE; MASS SPECTROMETRY; POLYMERS; RATE CONSTANTS; SIZE EXCLUSION CHROMATOGRAPHY; TITRATION; CHEMICAL ACTIVATION; EFFLUENT TREATMENT; ELECTROSPRAY IONIZATION; ENZYMES; INDUSTRIAL WASTE TREATMENT; INDUSTRIAL WASTES; INDUSTRIAL WATER TREATMENT; KINETICS; POLYSULFONES; WATER TREATMENT;

EID: 84896448424     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.03.002     Document Type: Article
Times cited : (25)

References (50)
  • 1
    • 84873723272 scopus 로고    scopus 로고
    • Insights into lignin degradation and its potential industrial applications
    • Abdel-Hamid A.M., Solbiati J.O., Cann I.K. Insights into lignin degradation and its potential industrial applications. Adv. Appl. Microbiol. 2013, 82:1-28.
    • (2013) Adv. Appl. Microbiol. , vol.82 , pp. 1-28
    • Abdel-Hamid, A.M.1    Solbiati, J.O.2    Cann, I.K.3
  • 2
    • 84888033757 scopus 로고    scopus 로고
    • Improvement of hydrogen peroxide stability of Pleurotus eryngii versatile ligninolytic peroxidase by rational protein engineering
    • Bao X., Huang X., Lu X., Li J.J. Improvement of hydrogen peroxide stability of Pleurotus eryngii versatile ligninolytic peroxidase by rational protein engineering. Enzyme Microb. Technol. 2014, 54:51-58.
    • (2014) Enzyme Microb. Technol. , vol.54 , pp. 51-58
    • Bao, X.1    Huang, X.2    Lu, X.3    Li, J.J.4
  • 3
    • 0038820029 scopus 로고    scopus 로고
    • Calorimetric determination of thermodynamic parameters of reaction reveals different enthalpic compensations of the yeast hexokinase isozymes
    • Bianconi M.L. Calorimetric determination of thermodynamic parameters of reaction reveals different enthalpic compensations of the yeast hexokinase isozymes. J. Biol. Chem. 2003, 278:18709-18713.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18709-18713
    • Bianconi, M.L.1
  • 4
    • 84883674268 scopus 로고    scopus 로고
    • The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase
    • Carabajal M., Kellner H., Levin L., Jehmlich N., Hofrichter M., Ullrich R. The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase. J. Biotechnol. 2013, 168:15-23.
    • (2013) J. Biotechnol. , vol.168 , pp. 15-23
    • Carabajal, M.1    Kellner, H.2    Levin, L.3    Jehmlich, N.4    Hofrichter, M.5    Ullrich, R.6
  • 7
    • 0042934024 scopus 로고    scopus 로고
    • Spectroscopic characteristics of ultrafiltration fractions of fulvic and humic acids isolated from an eucalyptus bleached Kraft pulp mill effluent
    • Duarte R.M.B.O., Santos E.B.H., Duarte A.C. Spectroscopic characteristics of ultrafiltration fractions of fulvic and humic acids isolated from an eucalyptus bleached Kraft pulp mill effluent. Water Res. 2003, 37:4073-4080.
    • (2003) Water Res. , vol.37 , pp. 4073-4080
    • Duarte, R.M.B.O.1    Santos, E.B.H.2    Duarte, A.C.3
  • 8
    • 84859420715 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidise using isothermal titration calorimetry: insights into manganese peroxidase activation and lignin peroxidase inhibition
    • Ertan H., Siddiqui K.S., Muenchhoff J., Charlton T., Cavicchioli R. Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidise using isothermal titration calorimetry: insights into manganese peroxidase activation and lignin peroxidase inhibition. Biochimie 2012, 94:1221-1231.
    • (2012) Biochimie , vol.94 , pp. 1221-1231
    • Ertan, H.1    Siddiqui, K.S.2    Muenchhoff, J.3    Charlton, T.4    Cavicchioli, R.5
  • 10
    • 0035671344 scopus 로고    scopus 로고
    • Synergistic effects of cellobiose dehydrogenase and manganese-dependent peroxidises during lignin degradation
    • Feng H., Jing F., Xuemei L.U., Peiji G.A.O., Jiaxiang C. Synergistic effects of cellobiose dehydrogenase and manganese-dependent peroxidises during lignin degradation. Chin. Sci. Bull. 2001, 46:1956-1961.
    • (2001) Chin. Sci. Bull. , vol.46 , pp. 1956-1961
    • Feng, H.1    Jing, F.2    Xuemei, L.U.3    Peiji, G.A.O.4    Jiaxiang, C.5
  • 12
    • 84877342330 scopus 로고    scopus 로고
    • Spectrophotometric analysis of fulvic acid solutions - a second look
    • Ghabbour E.A., Davies G. Spectrophotometric analysis of fulvic acid solutions - a second look. Ann. Environ. Sci. 2009, 3:131-138.
    • (2009) Ann. Environ. Sci. , vol.3 , pp. 131-138
    • Ghabbour, E.A.1    Davies, G.2
  • 13
    • 0032577520 scopus 로고    scopus 로고
    • A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
    • Heinfling A., Ruiz-Dueñas F.J., Martínez M.J., Bergbauer M., Szewzyk U., Martínez A.T. A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett. 1998, 428:141-146.
    • (1998) FEBS Lett. , vol.428 , pp. 141-146
    • Heinfling, A.1    Ruiz-Dueñas, F.J.2    Martínez, M.J.3    Bergbauer, M.4    Szewzyk, U.5    Martínez, A.T.6
  • 14
    • 0031010354 scopus 로고    scopus 로고
    • Depolymerization of low-rank coal by extracellular fungal systems. II. The ligninolytic enzymes of the coal-humic-acid-depolymerizing fungus Nematolomo frowardii b19
    • Hofrichter M., Fritsche W. Depolymerization of low-rank coal by extracellular fungal systems. II. The ligninolytic enzymes of the coal-humic-acid-depolymerizing fungus Nematolomo frowardii b19. Appl. Microbiol. Biotechnol. 1997, 47:419-424.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 419-424
    • Hofrichter, M.1    Fritsche, W.2
  • 15
    • 0030979258 scopus 로고    scopus 로고
    • Depolymerization of low-rank coal by extracellular fungal systems. III. In vitro depolymerisation of coal humic acids by crude preparation of manganese peroxidise from white-rot fungus Nematolomo frowardii b19
    • Hofrichter M., Fritsche W. Depolymerization of low-rank coal by extracellular fungal systems. III. In vitro depolymerisation of coal humic acids by crude preparation of manganese peroxidise from white-rot fungus Nematolomo frowardii b19. Appl. Microbiol. Biotechnol. 1997, 47:566-571.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 566-571
    • Hofrichter, M.1    Fritsche, W.2
  • 16
    • 33747079057 scopus 로고    scopus 로고
    • High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase
    • Lan J., Huang X., Hu M., Li Y., Qu Y., Gao P., Wu D. High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase. J. Biotechnol. 2006, 123:483-490.
    • (2006) J. Biotechnol. , vol.123 , pp. 483-490
    • Lan, J.1    Huang, X.2    Hu, M.3    Li, Y.4    Qu, Y.5    Gao, P.6    Wu, D.7
  • 17
    • 49149101569 scopus 로고    scopus 로고
    • Expanding the concepts in protein structure-function relationships and enzyme kinetics: teaching using morpheeins
    • Lawrence S.H., Jaffe E.K. Expanding the concepts in protein structure-function relationships and enzyme kinetics: teaching using morpheeins. Biochem. Mol. Biol. Educ. 2008, 36:274-283.
    • (2008) Biochem. Mol. Biol. Educ. , vol.36 , pp. 274-283
    • Lawrence, S.H.1    Jaffe, E.K.2
  • 18
    • 34547564903 scopus 로고    scopus 로고
    • Dynamic modeling of an enzymatic membrane reactor for the treatment of xenobiotic compounds
    • López C., Moreira M.T., Feijoo G., Lema J.M. Dynamic modeling of an enzymatic membrane reactor for the treatment of xenobiotic compounds. Biotechnol. Bioeng. 2007, 97:1128-1137.
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 1128-1137
    • López, C.1    Moreira, M.T.2    Feijoo, G.3    Lema, J.M.4
  • 19
    • 0036843595 scopus 로고    scopus 로고
    • UF of pulp and paper effluent: membrane fouling-prevention and cleaning
    • Maartens A., Jacobs E.P., Swart P. UF of pulp and paper effluent: membrane fouling-prevention and cleaning. J. Membr. Sci. 2002, 209:81-92.
    • (2002) J. Membr. Sci. , vol.209 , pp. 81-92
    • Maartens, A.1    Jacobs, E.P.2    Swart, P.3
  • 20
    • 79960809340 scopus 로고    scopus 로고
    • Industrial & biotechnological applications of ligninolytic enzymes of the basidiomycota: a review
    • Maciel M.J., Silva A.C., Ribeiro H.C.T. Industrial & biotechnological applications of ligninolytic enzymes of the basidiomycota: a review. Electron. J. Biotechnol. 2010, 13. 10.2225/vol13-issue6-fulltext-2.
    • (2010) Electron. J. Biotechnol. , vol.13
    • Maciel, M.J.1    Silva, A.C.2    Ribeiro, H.C.T.3
  • 22
    • 0032546787 scopus 로고    scopus 로고
    • Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese
    • Mester T., Field J.A. Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese. J. Biol. Chem. 1998, 273:15412-15417.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15412-15417
    • Mester, T.1    Field, J.A.2
  • 23
    • 84870381055 scopus 로고    scopus 로고
    • Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase
    • Morales M., Mate M.J., Romero A., Martínez M.J., Martínez Á.T., Ruiz-Dueñas F.J. Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase. J. Biol. Chem. 2012, 287:41053-41067.
    • (2012) J. Biol. Chem. , vol.287 , pp. 41053-41067
    • Morales, M.1    Mate, M.J.2    Romero, A.3    Martínez, M.J.4    Martínez, A.T.5    Ruiz-Dueñas, F.J.6
  • 24
    • 77954459285 scopus 로고    scopus 로고
    • An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases
    • Murphy L., Baumann M.J., Borch K., Sweeney M., Westh P. An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases. Anal. Biochem. 2010, 404:140-148.
    • (2010) Anal. Biochem. , vol.404 , pp. 140-148
    • Murphy, L.1    Baumann, M.J.2    Borch, K.3    Sweeney, M.4    Westh, P.5
  • 26
    • 42949084555 scopus 로고    scopus 로고
    • Springer, New York, USA, A. Pandey, C. Webb, C.R. Soccol, C. Larroche (Eds.)
    • Enzyme Technology 2006, Springer, New York, USA. A. Pandey, C. Webb, C.R. Soccol, C. Larroche (Eds.).
    • (2006) Enzyme Technology
  • 29
    • 67649799362 scopus 로고    scopus 로고
    • Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this
    • Ruiz-Dueñas F.J., Martínez A.T. Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this. Microb. Biotechnol. 2009, 2:164-177.
    • (2009) Microb. Biotechnol. , vol.2 , pp. 164-177
    • Ruiz-Dueñas, F.J.1    Martínez, A.T.2
  • 30
    • 33645841976 scopus 로고    scopus 로고
    • Monitoring of effluent DOM biodegradation using fluorescence UV and DOC measurements
    • Saadi I., Borisover M., Armon R., Laor Y. Monitoring of effluent DOM biodegradation using fluorescence UV and DOC measurements. Chemosphere 2006, 63:530-539.
    • (2006) Chemosphere , vol.63 , pp. 530-539
    • Saadi, I.1    Borisover, M.2    Armon, R.3    Laor, Y.4
  • 31
    • 0036913833 scopus 로고    scopus 로고
    • SEC-ICP-MS studies for elements binding to different molecular weight fractions of humic substances in compost extract obtained from urban solid waste
    • Sadi B.B.M., Wrobel K., Wrobel K., Kannamkumarath S.S., Castillo J.R., Caruso J.A. SEC-ICP-MS studies for elements binding to different molecular weight fractions of humic substances in compost extract obtained from urban solid waste. J. Environ. Monit. 2002, 4:1010-1016.
    • (2002) J. Environ. Monit. , vol.4 , pp. 1010-1016
    • Sadi, B.B.M.1    Wrobel, K.2    Wrobel, K.3    Kannamkumarath, S.S.4    Castillo, J.R.5    Caruso, J.A.6
  • 35
    • 78049429849 scopus 로고    scopus 로고
    • Humic substances fouling in ultrafiltration processes
    • Sutzkover-Gutman I., Hasson D., Semiat R. Humic substances fouling in ultrafiltration processes. Desalination 2010, 261:218-231.
    • (2010) Desalination , vol.261 , pp. 218-231
    • Sutzkover-Gutman, I.1    Hasson, D.2    Semiat, R.3
  • 36
    • 34447256086 scopus 로고    scopus 로고
    • Membrane independent limiting flux for RO and NF membranes fouled by humic acid
    • Tang C.Y., Leckie J.O. Membrane independent limiting flux for RO and NF membranes fouled by humic acid. Environ. Sci. Technol. 2007, 41:4767-4773.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 4767-4773
    • Tang, C.Y.1    Leckie, J.O.2
  • 37
    • 84896462505 scopus 로고    scopus 로고
    • Use of isothermal titration calorimetry to measure enzyme kinetics parameters
    • The Calorimetry Experts
    • The Calorimetry Experts Use of isothermal titration calorimetry to measure enzyme kinetics parameters. iTC Application Note 2003.
    • (2003) iTC Application Note
  • 38
    • 4043147145 scopus 로고    scopus 로고
    • Determination of molecular formulas and structural regularities of low molecular weight fulvic acids by size-exclusion chromatography with electrospray ionization quadrupole time-of-flight mass spectrometry
    • These A., Winkler M., Thomas C., Reemtsma T. Determination of molecular formulas and structural regularities of low molecular weight fulvic acids by size-exclusion chromatography with electrospray ionization quadrupole time-of-flight mass spectrometry. Rapid Commun. Mass. Spectrom. 2004, 18:1777-1786.
    • (2004) Rapid Commun. Mass. Spectrom. , vol.18 , pp. 1777-1786
    • These, A.1    Winkler, M.2    Thomas, C.3    Reemtsma, T.4
  • 39
    • 0031830472 scopus 로고    scopus 로고
    • In vitro degradation of insoluble lignin in aqueous media by lignin peroxidase and manganese peroxidase
    • Thompson D.N., Hames B.R., Reddy C.A., Grethlein H.E. In vitro degradation of insoluble lignin in aqueous media by lignin peroxidase and manganese peroxidase. Appl. Biochem. Biotechnol. 1998, 70-72:967-982.
    • (1998) Appl. Biochem. Biotechnol. , pp. 967-982
    • Thompson, D.N.1    Hames, B.R.2    Reddy, C.A.3    Grethlein, H.E.4
  • 40
    • 0035884687 scopus 로고    scopus 로고
    • Enzyme kinetics determined using calorimetry: a general assay for enzyme activity
    • Todd M.J., Gomez J. Enzyme kinetics determined using calorimetry: a general assay for enzyme activity. Anal. Biochem. 2001, 296:179-187.
    • (2001) Anal. Biochem. , vol.296 , pp. 179-187
    • Todd, M.J.1    Gomez, J.2
  • 41
    • 3042608648 scopus 로고    scopus 로고
    • Modeling kinetic data from in vitro drug metabolism enzyme experiments
    • Tracy T.S., Hummel M.A. Modeling kinetic data from in vitro drug metabolism enzyme experiments. Drug Metabol. Rev. 2004, 36:231-242.
    • (2004) Drug Metabol. Rev. , vol.36 , pp. 231-242
    • Tracy, T.S.1    Hummel, M.A.2
  • 43
    • 0026643601 scopus 로고
    • Oxidation of phenolic arylglycerol beta-aryl ether lignin model compounds by manganese peroxidase from Phanerochaete chrysosporium: oxidative cleavage of an alpha-carbonyl model compound
    • Tuor U., Wariishi H., Schoemaker H.E., Gold M.H. Oxidation of phenolic arylglycerol beta-aryl ether lignin model compounds by manganese peroxidase from Phanerochaete chrysosporium: oxidative cleavage of an alpha-carbonyl model compound. Biochemistry 1992, 31:4986-4995.
    • (1992) Biochemistry , vol.31 , pp. 4986-4995
    • Tuor, U.1    Wariishi, H.2    Schoemaker, H.E.3    Gold, M.H.4
  • 44
    • 27644580952 scopus 로고    scopus 로고
    • A comparative study on the photocatalytic degradation of humic substances of various origins
    • Uyguner C.S., Bekbolet M. A comparative study on the photocatalytic degradation of humic substances of various origins. Desalination 2005, 176:167-176.
    • (2005) Desalination , vol.176 , pp. 167-176
    • Uyguner, C.S.1    Bekbolet, M.2
  • 46
    • 84881543374 scopus 로고    scopus 로고
    • Biological pretreatment of corn stover with ligninolytic enzyme for highly efficient enzymatic hydrolysis
    • Wang F.-Q., Xie H., Chen W., Wang E.-T., Du F.-G., Song A.-D. Biological pretreatment of corn stover with ligninolytic enzyme for highly efficient enzymatic hydrolysis. Bioresour. Technol. 2013, 144:572-578.
    • (2013) Bioresour. Technol. , vol.144 , pp. 572-578
    • Wang, F.-Q.1    Xie, H.2    Chen, W.3    Wang, E.-T.4    Du, F.-G.5    Song, A.-D.6
  • 47
    • 67649888678 scopus 로고    scopus 로고
    • Structure and action mechanism of ligninolytic enzymes
    • Wong D.W.S. Structure and action mechanism of ligninolytic enzymes. Appl. Biochem. Biotechnol. 2009, 157:174-209.
    • (2009) Appl. Biochem. Biotechnol. , vol.157 , pp. 174-209
    • Wong, D.W.S.1
  • 48
    • 0024114522 scopus 로고
    • The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose
    • Woodward J., Lima M., Lee N.E. The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose. Biochem. J. 1988, 255:895-899.
    • (1988) Biochem. J. , vol.255 , pp. 895-899
    • Woodward, J.1    Lima, M.2    Lee, N.E.3
  • 49
    • 79960540516 scopus 로고    scopus 로고
    • Oxidation of polyaromatic hydrocarbons in systems containing water miscible organic solvents by the lignin peroxidase of Gleophyllum striatum MTCC-1117
    • Yadav M., Singh S.K., Sharma J.K., Yadav K.D. Oxidation of polyaromatic hydrocarbons in systems containing water miscible organic solvents by the lignin peroxidase of Gleophyllum striatum MTCC-1117. Environ. Technol. 2011, 32:1287-1294.
    • (2011) Environ. Technol. , vol.32 , pp. 1287-1294
    • Yadav, M.1    Singh, S.K.2    Sharma, J.K.3    Yadav, K.D.4
  • 50
    • 0017691462 scopus 로고
    • Regulation of pyruvate kinases from Fusarium oxysporum
    • Zink M.W. Regulation of pyruvate kinases from Fusarium oxysporum. Can. J. Microbiol. 1977, 23:1346-1359.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 1346-1359
    • Zink, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.