메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and β-ether lignin dimer

Author keywords

[No Author keywords available]

Indexed keywords

BENZYL ALCOHOL DERIVATIVE; COLORING AGENT; LIGNIN; PEROXIDASE; RECOMBINANT PROTEIN; VERATRYL ALCOHOL;

EID: 84942888204     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep08245     Document Type: Article
Times cited : (105)

References (37)
  • 1
    • 84878679101 scopus 로고    scopus 로고
    • Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum
    • Min, K. et al. Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum. Appl. Microbiol. Biotechnol. 97, 5627-5634(2013).
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 5627-5634
    • Min, K.1
  • 2
    • 77955658467 scopus 로고    scopus 로고
    • A biorefinery processing perspective: Treatment of lignocellulosic materials for the production of value-added products
    • FitzPatrick, M., Champagne, P., Cunningham, M. F. & Whitney, R. A. A biorefinery processing perspective: Treatment of lignocellulosic materials for the production of value-added products. Bioresour. Technol. 101, 8915-8922 (2010).
    • (2010) Bioresour. Technol. , vol.101 , pp. 8915-8922
    • FitzPatrick, M.1    Champagne, P.2    Cunningham, M.F.3    Whitney, R.A.4
  • 4
    • 0037015412 scopus 로고    scopus 로고
    • Ligninolytic enzymes of the fungus Irpex lacteus (Polyporus tulipiferae): Isolation and characterization of lignin peroxidase
    • Rothschild, N., Novotný, Č.,Šašek, V. & Dosoretz, C. G. Ligninolytic enzymes of the fungus Irpex lacteus (Polyporus tulipiferae): isolation and characterization of lignin peroxidase. Enzyme Microb. Technol. 31, 627-633 (2002).
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 627-633
    • Rothschild, N.1    Novotný, Č.2    Šašek, V.3    Dosoretz, C.G.4
  • 5
    • 67649786142 scopus 로고    scopus 로고
    • Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
    • Ruiz-Dueñas, F. J. et al. Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J. Exp. Bot. 60, 441-452 (2009).
    • (2009) J. Exp. Bot. , vol.60 , pp. 441-452
    • Ruiz-Dueñas, F.J.1
  • 6
    • 84871590888 scopus 로고    scopus 로고
    • Identification and Characterization of aMultifunctional Dye Peroxidase from a Lignin-Reactive Bacterium
    • Brown, M. E., Barros, T. & Chang, M. C. Y. Identification and Characterization of aMultifunctional Dye Peroxidase from a Lignin-Reactive Bacterium. ACS Chem. Biol. 7, 2074-2081 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , pp. 2074-2081
    • Brown, M.E.1    Barros, T.2    Chang, M.C.Y.3
  • 7
    • 0037117763 scopus 로고    scopus 로고
    • Review: Lignin conversion by manganese peroxidase (MnP)
    • Hofrichter, M. Review: lignin conversion by manganese peroxidase (MnP). Enzyme Microb. Technol. 30, 454-466 (2002).
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 454-466
    • Hofrichter, M.1
  • 8
    • 77957732425 scopus 로고    scopus 로고
    • Improving the simultaneous production of laccase and lignin peroxidase from Streptomyces lavendulae by medium optimization
    • Jing, D. Improving the simultaneous production of laccase and lignin peroxidase from Streptomyces lavendulae by medium optimization. Bioresour. Technol. 101, 7592-7597 (2010).
    • (2010) Bioresour. Technol. , vol.101 , pp. 7592-7597
    • Jing, D.1
  • 9
    • 0035821149 scopus 로고    scopus 로고
    • Comparison of two assay procedures for lignin peroxidase
    • Arora, D. S. & Gill, P. K. Comparison of two assay procedures for lignin peroxidase. Enzyme Microb.Technol. 28, 602-605 (2001).
    • (2001) Enzyme Microb.Technol. , vol.28 , pp. 602-605
    • Arora, D.S.1    Gill, P.K.2
  • 10
    • 4344686054 scopus 로고    scopus 로고
    • Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium
    • Ürek, R.Ö. & Pazarlioʇlu, N. K. Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium. Process Biochem. 39, 2061-2068 (2004).
    • (2004) Process Biochem. , vol.39 , pp. 2061-2068
    • Ürek, R.O.1    Pazarlioʇlu, N.K.2
  • 11
    • 79955761627 scopus 로고    scopus 로고
    • The emerging role for bacteria in lignin degradation and bio-product formation
    • Bugg, T. D. H., Ahmad, M., Hardiman, E. M. & Singh, R. The emerging role for bacteria in lignin degradation and bio-product formation. Curr. Opin. Biotechnol. 22, 394-400 (2011).
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 394-400
    • Bugg, T.D.H.1    Ahmad, M.2    Hardiman, E.M.3    Singh, R.4
  • 12
    • 79958856367 scopus 로고    scopus 로고
    • Identification of DypB from Rhodococcus jostii RHA1 as a Lignin Peroxidase
    • Ahmad, M. et al. Identification of DypB from Rhodococcus jostii RHA1 as a Lignin Peroxidase. Biochemistry 50, 5096-5107 (2011).
    • (2011) Biochemistry , vol.50 , pp. 5096-5107
    • Ahmad, M.1
  • 13
    • 77952368547 scopus 로고    scopus 로고
    • Development of novel assays for lignin degradation: Comparative analysis of bacterial and fungal lignin degraders
    • Ahmad, M. et al. Development of novel assays for lignin degradation: comparative analysis of bacterial and fungal lignin degraders. Mol. BioSyst. 6, 815-821 (2010).
    • (2010) Mol. BioSyst. , vol.6 , pp. 815-821
    • Ahmad, M.1
  • 14
    • 84871968243 scopus 로고    scopus 로고
    • Isolation and characterization of Streptomyces spp. Strains F-6 and F-7 capable of decomposing alkali lignin
    • Yang, Y. S., Zhou, J. T., Lu, H., Yuan, Y. L. & Zhao, L. H. Isolation and characterization of Streptomyces spp. strains F-6 and F-7 capable of decomposing alkali lignin. Environ. Technol. 33, 2603-2609 (2012).
    • (2012) Environ. Technol. , vol.33 , pp. 2603-2609
    • Yang, Y.S.1    Zhou, J.T.2    Lu, H.3    Yuan, Y.L.4    Zhao, L.H.5
  • 15
    • 84889669522 scopus 로고    scopus 로고
    • Isolation of Bacillus sp. Strains capable of decomposing alkali lignin and their application in combination with lactic acid bacteria for enhancing cellulase performance
    • Chang, Y.-C., Choi, D., Takamizawa, K. & Kikuchi, S. Isolation of Bacillus sp. strains capable of decomposing alkali lignin and their application in combination with lactic acid bacteria for enhancing cellulase performance. Bioresour. Technol. 152, 429-436 (2014).
    • (2014) Bioresour. Technol. , vol.152 , pp. 429-436
    • Chang, Y.-C.1    Choi, D.2    Takamizawa, K.3    Kikuchi, S.4
  • 16
    • 80053916434 scopus 로고    scopus 로고
    • Isolation and characterization of novel bacterial strains exhibiting ligninolytic potential
    • Bandounas, L., Wierckx, N., de Winde, J. & Ruijssenaars, H. Isolation and characterization of novel bacterial strains exhibiting ligninolytic potential. BMC Biotech. 11, 94 (2011).
    • (2011) BMC Biotech. , vol.11 , pp. 94
    • Bandounas, L.1    Wierckx, N.2    De Winde, J.3    Ruijssenaars, H.4
  • 17
    • 34248210185 scopus 로고    scopus 로고
    • Identification of low molecular weight aromatic compounds by gas chromatography-mass spectrometry (GC-MS) from kraft lignin degradation by three Bacillus sp
    • Raj, A., Krishna Reddy, M. M. & Chandra, R. Identification of low molecular weight aromatic compounds by gas chromatography-mass spectrometry (GC-MS) from kraft lignin degradation by three Bacillus sp. Int. Biodeterior. Biodegrad. 59, 292-296 (2007).
    • (2007) Int. Biodeterior. Biodegrad. , vol.59 , pp. 292-296
    • Raj, A.1    Krishna Reddy, M.M.2    Chandra, R.3
  • 18
    • 70349522119 scopus 로고    scopus 로고
    • Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase
    • Smith, A. T., Doyle, W. A., Dorlet, P. & Ivancich, A. Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase. Proc. Natl. Acad. Sci. 106, 16084-16089 (2009).
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 16084-16089
    • Smith, A.T.1    Doyle, W.A.2    Dorlet, P.3    Ivancich, A.4
  • 19
    • 3042846929 scopus 로고    scopus 로고
    • Electrochemical analysis of the interactions of laccase mediators with lignin model compounds
    • Bourbonnais, R., Leech, D. & Paice, M. G. Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim. Biophys. Acta, Gen. Subj. 1379, 381-390 (1998).
    • (1998) Biochim. Biophys. Acta, Gen. Subj. , vol.1379 , pp. 381-390
    • Bourbonnais, R.1    Leech, D.2    Paice, M.G.3
  • 21
    • 84868611010 scopus 로고    scopus 로고
    • Electrochemical study of vinylsulphone azo dye Reactive Black 5 and its determination at a glassy carbon electrode
    • Radi, A.,Mostafa, M. R., Hegazy, T. A. & Elshafey, R. M. Electrochemical study of vinylsulphone azo dye Reactive Black 5 and its determination at a glassy carbon electrode. J. Anal. Chem. 67, 890-894 (2012).
    • (2012) J. Anal. Chem. , vol.67 , pp. 890-894
    • Radi, A.1    Mostafa, M.R.2    Hegazy, T.A.3    Elshafey, R.M.4
  • 22
    • 77952889772 scopus 로고    scopus 로고
    • A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily
    • van Bloois, E., Torres Pazmiño, D., Winter, R. & Fraaije, M. A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl. Microbiol. Biotechnol. 86, 1419-1430 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1419-1430
    • Van Bloois, E.1    Torres Pazmiño, D.2    Winter, R.3    Fraaije, M.4
  • 23
    • 59649107848 scopus 로고    scopus 로고
    • Purification and Partial Characterization of Lignin Peroxidase from Acinetobacter calcoaceticus NCIM 2890 and Its Application in Decolorization of Textile Dyes
    • Ghodake, G., Kalme, S., Jadhav, J. & Govindwar, S. Purification and Partial Characterization of Lignin Peroxidase from Acinetobacter calcoaceticus NCIM 2890 and Its Application in Decolorization of Textile Dyes. Appl. Biochem. Biotechnol. 152, 6-14 (2009).
    • (2009) Appl. Biochem. Biotechnol. , vol.152 , pp. 6-14
    • Ghodake, G.1    Kalme, S.2    Jadhav, J.3    Govindwar, S.4
  • 24
    • 79961170376 scopus 로고    scopus 로고
    • Isolation and characterization of a fungus Aspergillus sp. Strain F-3 capable of degrading alkali lignin
    • Yang, Y. S., Zhou, J. T., Lu, H., Yuan, Y. L. & Zhao, L. H. Isolation and characterization of a fungus Aspergillus sp. strain F-3 capable of degrading alkali lignin. Biodegradation 22, 1017-1027 (2011).
    • (2011) Biodegradation , vol.22 , pp. 1017-1027
    • Yang, Y.S.1    Zhou, J.T.2    Lu, H.3    Yuan, Y.L.4    Zhao, L.H.5
  • 25
    • 84937576462 scopus 로고    scopus 로고
    • Screening, identification of lignin-degradating bacillus MN-8 and its characteristics in degradation of maize straw lignin
    • Li, H. Y., Li, S. N.,Wang, S. X.,Wang, Q. & Zhu, B. C. Screening, Identification of Lignin-Degradating Bacillus MN-8 and Its Characteristics in Degradation of Maize Straw Lignin. China Agric.Sci. 47, 324-333 (2014).
    • (2014) China Agric.Sci. , vol.47 , pp. 324-333
    • Li, H.Y.1    Li, S.N.2    Wang, S.X.3    Wang, Q.4    Zhu, B.C.5
  • 26
    • 84896691646 scopus 로고    scopus 로고
    • New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: Towards biotechnological applications
    • Santos, A.,Mendes, S., Brissos, V.&Martins, L. New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications. Appl. Microbiol. Biotechnol. 98, 2053-2065 (2014).
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 2053-2065
    • Santos, A.1    Mendes, S.2    Brissos, V.3    Martins, L.4
  • 27
    • 84870571391 scopus 로고    scopus 로고
    • Crystal structures of dyedecolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol
    • Yoshida, T., Tsuge, H., Hisabori, T. & Sugano, Y. Crystal structures of dyedecolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol. FEBS Lett. 586, 4351-4356 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 4351-4356
    • Yoshida, T.1    Tsuge, H.2    Hisabori, T.3    Sugano, Y.4
  • 28
    • 79959321050 scopus 로고    scopus 로고
    • The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
    • Yoshida, T., Tsuge, H., Konno, H., Hisabori, T. & Sugano, Y. The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue. FEBS J. 278, 2387-2394 (2011).
    • (2011) FEBS J. , vol.278 , pp. 2387-2394
    • Yoshida, T.1    Tsuge, H.2    Konno, H.3    Hisabori, T.4    Sugano, Y.5
  • 29
    • 0345472013 scopus 로고    scopus 로고
    • Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes
    • Kim, S. J. & Shoda, M. Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes. Appl.Environ.Microbiol. 65, 1029-1035 (1999).
    • (1999) Appl.Environ.Microbiol. , vol.65 , pp. 1029-1035
    • Kim, S.J.1    Shoda, M.2
  • 30
    • 72949091861 scopus 로고    scopus 로고
    • Molecular Characterization of a Novel Peroxidase from the Cyanobacterium Anabaena sp. Strain PCC 7120
    • Ogola, H. J. O. et al. Molecular Characterization of a Novel Peroxidase from the Cyanobacterium Anabaena sp. Strain PCC 7120. Appl. Environ. Microbiol. 75, 7509-7518 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7509-7518
    • Ogola, H.J.O.1
  • 31
    • 84900806554 scopus 로고    scopus 로고
    • Inactivating effect of phenolic unit structures on the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium
    • Thanh Mai Pham, L., Eom,M.-H. &Kim, Y. H. Inactivating effect of phenolic unit structures on the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium. Enzyme Microb. Technol. 61-62, 48-54 (2014).
    • (2014) Enzyme Microb. Technol. , vol.61-62 , pp. 48-54
    • Thanh Mai Pham, L.1    Eom, M.-H.2    Kim, Y.H.3
  • 32
    • 0036015837 scopus 로고    scopus 로고
    • Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes
    • Valderrama, B., Ayala, M. & Vazquez-Duhalt, R. Suicide Inactivation of Peroxidases and the Challenge of Engineering More Robust Enzymes. Chem. Biol. 9, 555-565 (2002).
    • (2002) Chem. Biol. , vol.9 , pp. 555-565
    • Valderrama, B.1    Ayala, M.2    Vazquez-Duhalt, R.3
  • 33
    • 84879834878 scopus 로고    scopus 로고
    • Characterization of a Novel Dye-Decolorizing Peroxidase (DyP)-Type Enzyme from Irpex lacteus and Its Application in Enzymatic Hydrolysis of Wheat Straw
    • Salvachúa, D., Prieto, A., Martínez,Á. T. & Martínez, M. J. Characterization of a Novel Dye-Decolorizing Peroxidase (DyP)-Type Enzyme from Irpex lacteus and Its Application in Enzymatic Hydrolysis of Wheat Straw. Appl. Environ. Microbiol. 79, 4316-4324 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4316-4324
    • Salvachúa, D.1    Prieto, A.2    Martínez, Á.T.3    Martínez, M.J.4
  • 34
    • 0033598740 scopus 로고    scopus 로고
    • Oligopeptidase B:ANew Type of Serine Peptidase with a Unique Substrate-Dependent Temperature Sensitivity
    • Polgár, L. Oligopeptidase B:ANew Type of Serine Peptidase with a Unique Substrate-Dependent Temperature Sensitivity. Biochemistry 38, 15548-15555 (1999).
    • (1999) Biochemistry , vol.38 , pp. 15548-15555
    • Polgár, L.1
  • 35
    • 5444224133 scopus 로고    scopus 로고
    • Predicting dye biodegradation from redox potentials
    • Zille, A. et al. Predicting Dye Biodegradation from Redox Potentials. Biotechnol.Progr. 20, 1588-1592 (2004).
    • (2004) Biotechnol.Progr. , vol.20 , pp. 1588-1592
    • Zille, A.1
  • 36
    • 0032577520 scopus 로고    scopus 로고
    • A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
    • Heinfling, A. et al. A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett. 428, 141-146 (1998).
    • (1998) FEBS Lett. , vol.428 , pp. 141-146
    • Heinfling, A.1
  • 37
    • 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. et al. Two Oxidation Sites for Low Redox Potential Substrates: A directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase. J. Biol. Chem. 287, 41053-41067 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 41053-41067
    • Morales, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.