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Volumn 44, Issue 1, 2013, Pages 291-297

Properties of catechol 1, 2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum

Author keywords

Anthracene; Biodegradation; Enzyme activity; Enzyme immobilization; Waste treatment

Indexed keywords

BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM FORTUITUM;

EID: 84879178407     PISSN: 15178382     EISSN: 16784405     Source Type: Journal    
DOI: 10.1590/S1517-83822013000100043     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 34547098835 scopus 로고    scopus 로고
    • Bioremediation and monitoring of aromatic-polluted habitats
    • Andreoni V, Gianfreda L (2007) Bioremediation and monitoring of aromatic-polluted habitats. App Microb Biotechnol 76:287-308.
    • (2007) App Microb Biotechnol , vol.76 , pp. 287-308
    • Andreoni, V.1    Gianfreda, L.2
  • 3
    • 0030977371 scopus 로고    scopus 로고
    • Ashton and Gabriele M. Siegel. Stimulation of spinach (Spinacia oleracea) chloroplast fructose-1,6-bisphosphatase by mercuric ions
    • Anthony R (1997) Ashton and Gabriele M. Siegel. Stimulation of spinach (Spinacia oleracea) chloroplast fructose-1,6-bisphosphatase by mercuric ions. FEBS Lett 408:30-32.
    • (1997) FEBS Lett , vol.408 , pp. 30-32
    • Anthony, R.1
  • 4
    • 0017184389 scopus 로고
    • A rapid e sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid e 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
  • 5
    • 0030809197 scopus 로고    scopus 로고
    • Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens
    • Briganti F, Pessione E, Giunta C, Scozzafava A (1997) Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens. FEBS Lett 416:61-64.
    • (1997) FEBS Lett , vol.416 , pp. 61-64
    • Briganti, F.1    Pessione, E.2    Giunta, C.3    Scozzafava, A.4
  • 8
    • 5344275196 scopus 로고    scopus 로고
    • Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13
    • Di Nardo G, Tilli S, Pessione E, Cavaletto M, Giunta C, Briganti F (2004) Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13. Arch Biochem Bioph 431:79-87.
    • (2004) Arch Biochem Bioph , vol.431 , pp. 79-87
    • Di Nardo, G.1    Tilli, S.2    Pessione, E.3    Cavaletto, M.4    Giunta, C.5    Briganti, F.6
  • 9
    • 0034613457 scopus 로고    scopus 로고
    • Potencial applicantions of oxidative enzyme and phenoloxidase-like compounds in wastewater and soil treatment: A review
    • Durán N, Esposito E (2000) Potencial applicantions of oxidative enzyme and phenoloxidase-like compounds in wastewater and soil treatment: A review. App Catalysis B 28:83-99.
    • (2000) App Catalysis B , vol.28 , pp. 83-99
    • Durán, N.1    Esposito, E.2
  • 10
    • 0034003045 scopus 로고    scopus 로고
    • Immobilization of functionally unstable catechol-2,3-dioxygenase greatly improves operational stability
    • Fernandez-Lafuente R, Guisan, J.M.; Ali, S.; Cowan, D. (2000) Immobilization of functionally unstable catechol-2,3-dioxygenase greatly improves operational stability. Enzyme Microb Tech 26:568-573.
    • (2000) Enzyme Microb Tech , vol.26 , pp. 568-573
    • Fernandez-Lafuente, R.1    Guisan, J.M.2    Ali, S.3    Cowan, D.4
  • 11
    • 59349114676 scopus 로고    scopus 로고
    • Catechol 1,2-dioxygenase from f-naphthol degrading thermophilic Geobacillus sp. strain: Purification and properties
    • Giedraityte G, Kalëdienë L (2009) Catechol 1,2-dioxygenase from f-naphthol degrading thermophilic Geobacillus sp. strain: Purification and properties. Cent Eur J Biol 4:68-73.
    • (2009) Cent Eur J Biol , vol.4 , pp. 68-73
    • Giedraityte, G.1    Kalëdienë, L.2
  • 12
    • 0026279083 scopus 로고
    • Authenticity and Reconstitution of Immobilized Enzymes: Characterization and Denaturation/ Renaturation of Glucoamylase II
    • Gottschalk N, Jaenicke R (1991) Authenticity and Reconstitution of Immobilized Enzymes: Characterization and Denaturation/ Renaturation of Glucoamylase II. Biotechnol Appl Bioc 14:324-335.
    • (1991) Biotechnol Appl Bioc , vol.14 , pp. 324-335
    • Gottschalk, N.1    Jaenicke, R.2
  • 13
    • 0013892853 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida
    • Hegman GD (1966) Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. J Bacteriol. 91:1140-1154.
    • (1966) J Bacteriol. , vol.91 , pp. 1140-1154
    • Hegman, G.D.1
  • 14
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization-Aqueous and non-aqueous environment
    • Iyer PV, Ananthanarayan L (2008) Enzyme stability and stabilization-Aqueous and non-aqueous environment. Process Biochem 43:1019-1032.
    • (2008) Process Biochem , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 15
    • 33847240147 scopus 로고    scopus 로고
    • Characterization of a polycyclic aromatic hydrocarbon-degrading microbial consortium from a petrochemical sludge landfarming site
    • Jacques RJS, Okeke BC, Bento FM, Peralba MCR, Camargo FAO (2007) Characterization of a polycyclic aromatic hydrocarbon-degrading microbial consortium from a petrochemical sludge landfarming site. Bioremed J 11:1-11.
    • (2007) Bioremed J , vol.11 , pp. 1-11
    • Jacques, R.J.S.1    Okeke, B.C.2    Bento, F.M.3    Peralba, M.C.R.4    Camargo, F.A.O.5
  • 17
    • 16644396090 scopus 로고    scopus 로고
    • Principles of microbial PAH-degradation in soil
    • Johnsen AR, Wick LY, Harms H (2005) Principles of microbial PAH-degradation in soil. Environ Pollut 133:71-84.
    • (2005) Environ Pollut , vol.133 , pp. 71-84
    • Johnsen, A.R.1    Wick, L.Y.2    Harms, H.3
  • 18
    • 13844298122 scopus 로고    scopus 로고
    • Interfacial effects in a twophase partitioning bioreactor: Gedradation ps polycyclic aromatic hydrocarbons (PAHs) by a hydrophobic Mycobacterium
    • Macleod CT, Daugulis AJ (2005) Interfacial effects in a twophase partitioning bioreactor: Gedradation ps polycyclic aromatic hydrocarbons (PAHs) by a hydrophobic Mycobacterium. Process Biochem 40:1799-1805.
    • (2005) Process Biochem , vol.40 , pp. 1799-1805
    • McLeod, C.T.1    Daugulis, A.J.2
  • 19
    • 33746109598 scopus 로고    scopus 로고
    • Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels
    • Kalogeris E, Sanakis Y, Mamma D, Christakopoulos P, Kekos D, Stamatis H (2006) Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels. Enzyme Microb Tech 39:1113-1121.
    • (2006) Enzyme Microb Tech , vol.39 , pp. 1113-1121
    • Kalogeris, E.1    Sanakis, Y.2    Mamma, D.3    Christakopoulos, P.4    Kekos, D.5    Stamatis, H.6
  • 20
    • 0014408669 scopus 로고
    • Mercury(II) stimulation of malate dehydrogenase activity
    • Karamitsu HK (1968) Mercury(II) stimulation of malate dehydrogenase activity. The J Biol Chem 243:1016-1021.
    • (1968) The J Biol Chem , vol.243 , pp. 1016-1021
    • Karamitsu, H.K.1
  • 21
    • 0020054928 scopus 로고
    • Rapid screen for bacteria degrading water-insoluble, solid hydrocarbons on agar plates
    • Kiyohara H, Nagao K, Yana K (1982) Rapid screen for bacteria degrading water-insoluble, solid hydrocarbons on agar plates. Appl Environ Microbiol 43:454-457.
    • (1982) Appl Environ Microbiol , vol.43 , pp. 454-457
    • Kiyohara, H.1    Nagao, K.2    Yana, K.3
  • 22
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin and chitosan based materials for enzyme immobilizations: A review
    • Krajewska B (2004) Application of chitin and chitosan based materials for enzyme immobilizations: A review. Enzyme Microb Tech 35:126-139.
    • (2004) Enzyme Microb Tech , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 24
    • 0034111128 scopus 로고    scopus 로고
    • Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment
    • Mateo C, Abian O, Fernandez-Lafuente R, Guisan JM (2000) Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment. Enzyme Microb Tech 26:509-515.
    • (2000) Enzyme Microb Tech , vol.26 , pp. 509-515
    • Mateo, C.1    Abian, O.2    Fernandez-Lafuente, R.3    Guisan, J.M.4
  • 25
    • 4544313536 scopus 로고    scopus 로고
    • Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22
    • Matsumura E, Ooi S, Murakami S, Takenaka S, Aoki K (2004) Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22. J Biosci Bioeng 98:71-76.
    • (2004) J Biosci Bioeng , vol.98 , pp. 71-76
    • Matsumura, E.1    Ooi, S.2    Murakami, S.3    Takenaka, S.4    Aoki, K.5
  • 26
    • 68649126067 scopus 로고    scopus 로고
    • Calcium alginate-starch hybrid support for both surface immobilization and entrapment of bitter gourd (Momordica charantia) peroxidase
    • Matto M, Husain Q (2009) Calcium alginate-starch hybrid support for both surface immobilization and entrapment of bitter gourd (Momordica charantia) peroxidase. J Mol Catal. B-Enzym 57:164-170.
    • (2009) J Mol Catal. B-Enzym , vol.57 , pp. 164-170
    • Matto, M.1    Husain, Q.2
  • 27
    • 0032143496 scopus 로고    scopus 로고
    • PuriWcation and characterization of four catechol 1,2-dioxygenase isozymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17
    • Murakami S, Wang CL, Naito A, Shinke R, Aoki K (1998) PuriWcation and characterization of four catechol 1,2-dioxygenase isozymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17. Microbiol Res 153:163-171.
    • (1998) Microbiol Res , vol.153 , pp. 163-171
    • Murakami, S.1    Wang, C.L.2    Naito, A.3    Shinke, R.4    Aoki, K.5
  • 28
    • 79952283769 scopus 로고    scopus 로고
    • Performance improvement of araujiain, a cystein phytoprotease, by immobilization within calcium alginate beads
    • Quiroga E, Illane S CO, Ochoa NA. Barberis, S. (2011). Performance improvement of araujiain, a cystein phytoprotease, by immobilization within calcium alginate beads. Process Biochem. 46:1029-1034.
    • (2011) Process Biochem. , vol.46 , pp. 1029-1034
    • Quiroga, E.1    Illane, S.C.O.2    Ochoa, N.A.3    Barberis, S.4
  • 29
    • 0344234325 scopus 로고    scopus 로고
    • Hydrolysis of starch by a mixture of glucoamylase and pullulanase entrapped individually in calcium alginate beads
    • Roy I, Gupta NM (2004) Hydrolysis of starch by a mixture of glucoamylase and pullulanase entrapped individually in calcium alginate beads. Enzyme Microb Technol 34:26-32.
    • (2004) Enzyme Microb Technol , vol.34 , pp. 26-32
    • Roy, I.1    Gupta, N.M.2
  • 31
    • 33847126079 scopus 로고    scopus 로고
    • Purification and characterization of a catochel 1,2-dioxygenase from a phenol degrading Candida albicans TL3
    • Tsai SC, Li YK (2007) Purification and characterization of a catochel 1,2-dioxygenase from a phenol degrading Candida albicans TL3. Arch Microbiol 187:199-206.
    • (2007) Arch Microbiol , vol.187 , pp. 199-206
    • Tsai, S.C.1    Li, Y.K.2
  • 32
    • 33646540690 scopus 로고    scopus 로고
    • Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source
    • Wang CL, You SL, Wang SL (2006) Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Process Biochem 41:1594-1601.
    • (2006) Process Biochem , vol.41 , pp. 1594-1601
    • Wang, C.L.1    You, S.L.2    Wang, S.L.3
  • 33
    • 0035862144 scopus 로고    scopus 로고
    • Kinetics of mass transfer-limited bacterial grownth on solid PAHs
    • Wick LY, Colangelo T, Harms H (2001) Kinetics of mass transfer-limited bacterial grownth on solid PAHs. Environ Sci Tech 35:354-361.
    • (2001) Environ Sci Tech , vol.35 , pp. 354-361
    • Wick, L.Y.1    Colangelo, T.2    Harms, H.3
  • 34
    • 28844495397 scopus 로고    scopus 로고
    • Enzyme technology and biological remediation
    • Whiteley CG, Lee JD (2006) Enzyme technology and biological remediation. Enzyme Microb Tech 38:291-316.
    • (2006) Enzyme Microb Tech , vol.38 , pp. 291-316
    • Whiteley, C.G.1    Lee, J.D.2
  • 35
    • 0033118523 scopus 로고    scopus 로고
    • Removal of benzene in a hybrid bioreactor
    • Yeom SH, Yoo YJ (1999) Removal of benzene in a hybrid bioreactor. Process Biochem 34:281-88.
    • (1999) Process Biochem , vol.34 , pp. 281-288
    • Yeom, S.H.1    Yoo, Y.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.