Catechol 1,2-dioxygenase from α-naphthol degrading thermophilic Geobacillus sp. strain: purification and properties

Giedraityte, G.B.; Kalėdienė, Lilija

doi:10.2478/s11535-008-0049-y

Cited by 15 publications

(13 citation statements)

References 22 publications

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“…AN-22 and Arthrobacter species BA-5-17, respectively. Giedraityte and Kalediene (2009) reported only 27 and 6 % of the relative activity to catechol (7.42 U/mg of protein) of a catechol 1,2-dioxygenase from Geobacillus sp. towards 3-methylcatechol and 4-methylcatechol, respectively.…”

Section: Resultsmentioning

confidence: 99%

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

Guzik

Hupert-Kocurek

Sitnik

et al. 2013

Antonie van Leeuwenhoek

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This is the first report of a catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 °C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of Km and Vmax was 12.8 μM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2-dioxygenase we observed substrate inhibition at >80 μM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2-dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives.

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Section: Resultsmentioning

confidence: 99%

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

Guzik

Hupert-Kocurek

Sitnik

et al. 2013

Antonie van Leeuwenhoek

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“…Cu 2+ drastically inhibited the C12O enzyme activity produced by P. putida (Wang et al , 2006), Geobacillus sp. (Giedraityte and Kalëdienë, 2009) and Alcaligenes xylosoxidans (Yeom and Yoo, 1999). However, the inhibition was lower than that showed by these authors, mainly by the immobilized enzyme.…”

Section: Discussionmentioning

confidence: 99%

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

Silva

Jacques

Andreazza

et al. 2013

Braz. J. Microbiol.

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Polycyclic aromatic hydrocarbons (PAH) are carcinogenic compounds which contaminate water and soil, and the enzymes can be used for bioremediation of these environments. This study aimed to evaluate some environmental conditions that affect the production and activity of the catechol 1,2-dioxygenase (C12O) by Mycobacterium fortuitum in the cell free and immobilized extract in sodium alginate. The bacterium was grown in mineral medium and LB broth containing 250 mg L−1 of anthracene (PAH). The optimum conditions of pH (4.0–9.0), temperature (5–70 °C), reaction time (10–90 min) and the effect of ions in the enzyme activity were determined. The Mycobacterium cultivated in LB shown higher growth and the C12O activity was two-fold higher to that in the mineral medium. To both extracts the highest enzyme activity was at pH 8.0, however, the immobilized extract promoted the increase in the C12O activity in a pH range between 4.0 and 8.5. The immobilized extract increased the enzymatic activity time and showed the highest C12O activity at 45 °C, 20 °C higher than the greatest temperature in the cell free extract. The enzyme activity in both extracts was stimulated by Fe3+, Hg2+ and Mn2+ and inhibited by NH4+ and Cu2+, but the immobilization protected the enzyme against the deleterious effects of K+ and Mg2+ in tested concentrations. The catechol 1,2-dioxygenase of Mycobacterium fortuitum in the immobilized extract has greater stability to the variations of pH, temperature and reaction time, and show higher activity in presence of ions, comparing to the cell free extract.

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“…21 One milliliter of cell-free extract (9000 U) was suspended in 9 mL of 2% (w/v) sodium alginate prepared in 50 mM Tris-HCl buffer solution (pH 8.0). After homogenization of the mixture, the enzyme was dripped into 100 mL of solution of 0.2 M of CaCl 2 , using a pipette.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans

Silva¹,

Camargo²,

Andreazza³

et al. 2012

Quím. Nova

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Recebido em 23/1/12; aceito em 23/4/12; publicado na web em 20/7/2012 This study aimed to evaluate the environmental conditions for enzyme activity of catechol 1,2-dioxygenase (C1,2O) and catechol 2,3-dioxygenase (C2,3O) produced by Gordonia polyisoprenivorans in cell-free and immobilized extracts. The optimum conditions of pH, temperature, time course and effect of ions for enzyme activity were determined. Peak activity of C1,2O occurred at pH 8.0. The isolate exhibited the highest activity of C2,3O at pH 7.0 and 8.0 for the cell-free extract and immobilized extract, respectively. This isolate exhibited important characteristics such as broad range of pH, temperature and time course for enzyme activity.

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Catechol 1,2-dioxygenase from α-naphthol degrading thermophilic Geobacillus sp. strain: purification and properties

Cited by 15 publications

References 22 publications

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

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

Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans

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