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pseudomonas putida trevisan migula mnb1  (ATCC)


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    Structured Review

    ATCC pseudomonas putida trevisan migula mnb1
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula Mnb1, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation"

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    Journal: Life

    doi: 10.3390/life14020171

    Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Figure Legend Snippet: Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Techniques Used: Comparison, Sequencing



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    94
    ATCC pseudomonas putida trevisan migula mnb1
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula Mnb1, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pseudomonas putida trevisan migula mnb1/product/ATCC
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    ATCC cultivation p putida trevisan migula
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Cultivation P Putida Trevisan Migula, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC pseudomonas putida trevisan migula
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC pseudomonas putida trevisan migula p2 atcc 2557
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula P2 Atcc 2557, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC pseudomonas putida trevisan migula p2 atcc 25571
    Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula P2 Atcc 25571, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC ccug 25571
    The indicated P. intermedia strains, as well as A) M. catarrhalis RH 4, P. gingivalis W50 and W83 (C4BP binding positive controls), M. catarrhalis Δ uspA 1/2, and E. coli DH5α (C4BP binding negative controls) or B) S. pyogenes <t>CCUG</t> <t>25571</t> (FH binding positive control), S. aureus ATCC 25923, and E. coli DH5α (FH binding negative controls) were mixed with (A) 500 kcpm 125 I-C4BP or (B) 125 I-FH and incubated for 1 h at RT. Proteins bound to bacteria were detected as described in . Samples containing 125 I-labeled proteins that were incubated with buffer alone served as negative controls. Bars represent averages of three independent experiments performed in duplicates and SD are indicated as error bars. One-way ANOVA and Tukey's post-hoc test was used for statistical analysis as compared to negative controls (*** p<0.001; * p<0.05; n.s., not significant).
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    ATCC mutans strains atcc 15175
    The indicated P. intermedia strains, as well as A) M. catarrhalis RH 4, P. gingivalis W50 and W83 (C4BP binding positive controls), M. catarrhalis Δ uspA 1/2, and E. coli DH5α (C4BP binding negative controls) or B) S. pyogenes <t>CCUG</t> <t>25571</t> (FH binding positive control), S. aureus ATCC 25923, and E. coli DH5α (FH binding negative controls) were mixed with (A) 500 kcpm 125 I-C4BP or (B) 125 I-FH and incubated for 1 h at RT. Proteins bound to bacteria were detected as described in . Samples containing 125 I-labeled proteins that were incubated with buffer alone served as negative controls. Bars represent averages of three independent experiments performed in duplicates and SD are indicated as error bars. One-way ANOVA and Tukey's post-hoc test was used for statistical analysis as compared to negative controls (*** p<0.001; * p<0.05; n.s., not significant).
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    ATCC pseudomonas putida atcc 17453
    The indicated P. intermedia strains, as well as A) M. catarrhalis RH 4, P. gingivalis W50 and W83 (C4BP binding positive controls), M. catarrhalis Δ uspA 1/2, and E. coli DH5α (C4BP binding negative controls) or B) S. pyogenes <t>CCUG</t> <t>25571</t> (FH binding positive control), S. aureus ATCC 25923, and E. coli DH5α (FH binding negative controls) were mixed with (A) 500 kcpm 125 I-C4BP or (B) 125 I-FH and incubated for 1 h at RT. Proteins bound to bacteria were detected as described in . Samples containing 125 I-labeled proteins that were incubated with buffer alone served as negative controls. Bars represent averages of three independent experiments performed in duplicates and SD are indicated as error bars. One-way ANOVA and Tukey's post-hoc test was used for statistical analysis as compared to negative controls (*** p<0.001; * p<0.05; n.s., not significant).
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    94
    ATCC strain p putida f1
    Schematic representation of bioreactor/recovery loop used for biotransformation . (a) Two-step bioreactor/recovery loop used for biotransformation of 3-nitrophenol to 3-nitrocatechol by strain P. <t>putida</t> <t>F1.</t> (b) Single- step bioreactor/recovery loop used for biotransformation of toluene to 3-methylcatechol by E. coli expression clone (pDTG602).
    Strain P Putida F1, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Journal: Life

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    doi: 10.3390/life14020171

    Figure Lengend Snippet: Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Article Snippet: Cultures of Pseudomonas putida (Trevisan) Migula MnB1 supplied by American Type Culture Collection (ATCC #23483) were prepared and grown at room temperature or 30 °C for 3 days.

    Techniques: Comparison, Sequencing

    The indicated P. intermedia strains, as well as A) M. catarrhalis RH 4, P. gingivalis W50 and W83 (C4BP binding positive controls), M. catarrhalis Δ uspA 1/2, and E. coli DH5α (C4BP binding negative controls) or B) S. pyogenes CCUG 25571 (FH binding positive control), S. aureus ATCC 25923, and E. coli DH5α (FH binding negative controls) were mixed with (A) 500 kcpm 125 I-C4BP or (B) 125 I-FH and incubated for 1 h at RT. Proteins bound to bacteria were detected as described in . Samples containing 125 I-labeled proteins that were incubated with buffer alone served as negative controls. Bars represent averages of three independent experiments performed in duplicates and SD are indicated as error bars. One-way ANOVA and Tukey's post-hoc test was used for statistical analysis as compared to negative controls (*** p<0.001; * p<0.05; n.s., not significant).

    Journal: PLoS ONE

    Article Title: Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

    doi: 10.1371/journal.pone.0034852

    Figure Lengend Snippet: The indicated P. intermedia strains, as well as A) M. catarrhalis RH 4, P. gingivalis W50 and W83 (C4BP binding positive controls), M. catarrhalis Δ uspA 1/2, and E. coli DH5α (C4BP binding negative controls) or B) S. pyogenes CCUG 25571 (FH binding positive control), S. aureus ATCC 25923, and E. coli DH5α (FH binding negative controls) were mixed with (A) 500 kcpm 125 I-C4BP or (B) 125 I-FH and incubated for 1 h at RT. Proteins bound to bacteria were detected as described in . Samples containing 125 I-labeled proteins that were incubated with buffer alone served as negative controls. Bars represent averages of three independent experiments performed in duplicates and SD are indicated as error bars. One-way ANOVA and Tukey's post-hoc test was used for statistical analysis as compared to negative controls (*** p<0.001; * p<0.05; n.s., not significant).

    Article Snippet: Likewise, S. pyogenes CCUG 25571 (FH binding positive control) and S. aureus ATCC 25923 and E. coli DH5α (FH binding negative controls) appeared to be appropriate internal controls investigating FH acquisition by P. intermedia .

    Techniques: Binding Assay, Positive Control, Incubation, Labeling

    Schematic representation of bioreactor/recovery loop used for biotransformation . (a) Two-step bioreactor/recovery loop used for biotransformation of 3-nitrophenol to 3-nitrocatechol by strain P. putida F1. (b) Single- step bioreactor/recovery loop used for biotransformation of toluene to 3-methylcatechol by E. coli expression clone (pDTG602).

    Journal: BMC Biotechnology

    Article Title: A process optimization for bio-catalytic production of substituted catechols (3-nitrocatechol and 3-methylcatechol

    doi: 10.1186/1472-6750-10-49

    Figure Lengend Snippet: Schematic representation of bioreactor/recovery loop used for biotransformation . (a) Two-step bioreactor/recovery loop used for biotransformation of 3-nitrophenol to 3-nitrocatechol by strain P. putida F1. (b) Single- step bioreactor/recovery loop used for biotransformation of toluene to 3-methylcatechol by E. coli expression clone (pDTG602).

    Article Snippet: Strain P. putida F1 (ATCC No. 700007) was procured from American Type Culture Collection (ATCC) , USA.

    Techniques: Expressing

    HPLC analysis showing accumulation of 3-substituted catechols . (a) Standard compounds of 3-nitrophenol and 3-nitrocatechol. ( b) Minimal medium containing 3-nitrophenol showing accumulation of 3-nitrocatechol in the medium by strain P. putida F1. (c) Standard compound of 3-methylcatechol. (d) Minimal medium containing toluene showing accumulation of 3-methylcatechol in the medium by E. coli expression clone (pDTG602).

    Journal: BMC Biotechnology

    Article Title: A process optimization for bio-catalytic production of substituted catechols (3-nitrocatechol and 3-methylcatechol

    doi: 10.1186/1472-6750-10-49

    Figure Lengend Snippet: HPLC analysis showing accumulation of 3-substituted catechols . (a) Standard compounds of 3-nitrophenol and 3-nitrocatechol. ( b) Minimal medium containing 3-nitrophenol showing accumulation of 3-nitrocatechol in the medium by strain P. putida F1. (c) Standard compound of 3-methylcatechol. (d) Minimal medium containing toluene showing accumulation of 3-methylcatechol in the medium by E. coli expression clone (pDTG602).

    Article Snippet: Strain P. putida F1 (ATCC No. 700007) was procured from American Type Culture Collection (ATCC) , USA.

    Techniques: Expressing

    Optimization of different conditions at laboratory scale shake flask (250 ml) . (a) Different media compositions used for the production of 3-nitrocatechol from 3-nitrophenol by strain P. putida F1. (b) pH of the medium. (c) Aeration. (d) Temperature. (e) 3-nitrophenol concentration. (f) Inoculums size. (g) Different media compositions used for the production of 3-methylcatechol from toluene by E. coli expression clone (pDTG602). (h) pH of the medium. (i) Temperature. (j) Aeration.

    Journal: BMC Biotechnology

    Article Title: A process optimization for bio-catalytic production of substituted catechols (3-nitrocatechol and 3-methylcatechol

    doi: 10.1186/1472-6750-10-49

    Figure Lengend Snippet: Optimization of different conditions at laboratory scale shake flask (250 ml) . (a) Different media compositions used for the production of 3-nitrocatechol from 3-nitrophenol by strain P. putida F1. (b) pH of the medium. (c) Aeration. (d) Temperature. (e) 3-nitrophenol concentration. (f) Inoculums size. (g) Different media compositions used for the production of 3-methylcatechol from toluene by E. coli expression clone (pDTG602). (h) pH of the medium. (i) Temperature. (j) Aeration.

    Article Snippet: Strain P. putida F1 (ATCC No. 700007) was procured from American Type Culture Collection (ATCC) , USA.

    Techniques: Concentration Assay, Expressing

    Induced and un-induced conditions for production of 3-substituted catechols . (a) Production of 3-nitrocatechol from 3-nitrophenol by strain P. putida F1 under induced (--■--) and un-induced (--●--) conditions. (b) Production of 3-methylcatechol from toluene by E. coli expression clone (pDTG602) under induced (--■--) and un-induced (--●--) conditions.

    Journal: BMC Biotechnology

    Article Title: A process optimization for bio-catalytic production of substituted catechols (3-nitrocatechol and 3-methylcatechol

    doi: 10.1186/1472-6750-10-49

    Figure Lengend Snippet: Induced and un-induced conditions for production of 3-substituted catechols . (a) Production of 3-nitrocatechol from 3-nitrophenol by strain P. putida F1 under induced (--■--) and un-induced (--●--) conditions. (b) Production of 3-methylcatechol from toluene by E. coli expression clone (pDTG602) under induced (--■--) and un-induced (--●--) conditions.

    Article Snippet: Strain P. putida F1 (ATCC No. 700007) was procured from American Type Culture Collection (ATCC) , USA.

    Techniques: Expressing

    3-substituted catechols at pilot scale . (a) 3-nitrocatechol production (◆) with concomitant depletion of 3-nitrophenol (□) by strain P. putida F1. (b) 3-methylcatechol production (■) from toluene by E. coli expression clone (pDTG602).

    Journal: BMC Biotechnology

    Article Title: A process optimization for bio-catalytic production of substituted catechols (3-nitrocatechol and 3-methylcatechol

    doi: 10.1186/1472-6750-10-49

    Figure Lengend Snippet: 3-substituted catechols at pilot scale . (a) 3-nitrocatechol production (◆) with concomitant depletion of 3-nitrophenol (□) by strain P. putida F1. (b) 3-methylcatechol production (■) from toluene by E. coli expression clone (pDTG602).

    Article Snippet: Strain P. putida F1 (ATCC No. 700007) was procured from American Type Culture Collection (ATCC) , USA.

    Techniques: Expressing