Improved catalytic activities of a dye-decolorizing peroxidase (DyP) by overexpression of ALA and heme biosynthesis genes in Escherichia coli

Ramzi, Ahmad Bazli; Hyeon, Jeong Eun; Han, Sung Ok

doi:10.1016/j.procbio.2015.05.004

Cited by 19 publications

(6 citation statements)

References 45 publications

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“…Under acidic conditions at pH 3.5, Il -DyP4 was more robust for ABTS oxidation, which fell within the optimal pH range (pH 3–4.5) of most of the DyPs reported from fungi (Linde et al 2014 ; Fernández-Fueyo et al 2015 ; Behrens et al 2016 ), and was similar to the optimal pH of native DyP from I. lacteus (Salvachúa et al 2013 ). Intriguingly, compared with the acidic pH of fungi DyPs, the optimal pH of bacteria DyPs was 5.0–7.0 (Yu et al 2014 ; Ramzi et al 2015 ; Rahmanpour et al 2016 ). The most distinguishing feature of DyP peroxidases is their powerful catalytic properties (Colpa et al 2014 ).…”

Section: Discussionmentioning

confidence: 99%

Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

et al. 2018

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Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce. Recently, the genome sequencing and annotation of this strain provided comprehensive picture of the ligninolytic peroxidase gene family. In addition to revealing the presence of 13 MnPs, genes for five dye-decolorizing peroxidases (DyPs) were also discovered in the I. lacteus F17 genome, which are unrelated to the fungal class II peroxidases. In the present study, amino acid sequences of five DyPs and 13 MnPs, representing two different families of heme peroxidases, were analyzed. Of these, two enzymes, a DyP (Il-DyP4) and a MnP (Il-MnP6) were expressed respectively in Escherichia coli, and were characterized by comparing their molecular models, substrate specificities, and catalytic features. The results showed that Il-DyP4 possessed a higher catalytic efficiency for some representative substrates, and a stronger decolorizing ability to a wide range of synthetic dyes in acidic conditions. Based on electrochemical measurements, Il-DyP4 was found to have a high redox potential of 27 mV at pH 3.5, which was superior to that of Il-MnP6 (− 75 mV), thereby contributing to its ability to oxidize high redox potential substrates, such as veratryl alcohol and polymeric dye Poly R-478. The results highlighted the potential of Il-DyP4 for use in industrial and environmental applications.Electronic supplementary materialThe online version of this article (10.1186/s13568-018-0648-6) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

et al. 2018

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“…Laboratory E. coli strains are often unable to import or synthesize enough heme for highly overexpressed heme enzymes [22,30,31]. In this work we tried to circumvent this problem by lowering the expression level of the enzyme or through the expression of TfuDyP in alternative E. coli strains.…”

Section: Discussionmentioning

confidence: 99%

High overexpression of dye decolorizing peroxidase TfuDyP leads to the incorporation of heme precursor protoporphyrin IX

Colpa

Fraaije

2016

Journal of Molecular Catalysis B: Enzymatic

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“…Corynebacterium glutamicum , a gram-positive, nonpathogenic and facultative anaerobic organism, has been frequently used and developed for large-scale production of a variety of amino acids such as l -glutamate and l -lysine, proteins, and monomers for various chemical compounds from renewable biomass 26 – 31 . Recently, we reported that the engineered C. glutamicum produced ALA, a precursor in the heme biosynthesis pathway 32 , 33 . ALA biosynthesis in almost all bacteria containing Escherichia coli and C. glutamicum is the rate-limiting step in the heme biosynthesis pathway 34 – 36 .…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of organic photosensitizer Zn-porphyrin by diphtheria toxin repressor (DtxR)-mediated global upregulation of engineered heme biosynthesis pathway in Corynebacterium glutamicum

Joo

Hyeon

et al. 2018

Sci Rep

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Zn-porphyrin is a promising organic photosensitizer in various fields including solar cells, interface and biomedical research, but the biosynthesis study has been limited, probably due to the difficulty of understanding complex biosynthesis pathways. In this study, we developed a Corynebacterium glutamicum platform strain for the biosynthesis of Zn-coproporphyrin III (Zn-CP III), in which the heme biosynthesis pathway was efficiently upregulated. The pathway was activated and reinforced by strong promoter-induced expression of hemAM (encoding mutated glutamyl-tRNA reductase) and hemL (encoding glutamate-1-semialdehyde aminotransferase) genes. This engineered strain produced 33.54 ± 3.44 mg/l of Zn-CP III, while the control strain produced none. For efficient global regulation of the complex pathway, the dtxR gene encoding the transcriptional regulator diphtheria toxin repressor (DtxR) was first overexpressed in C. glutamicum with hemAM and hemL genes, and its combinatorial expression was improved by using effective genetic tools. This engineered strain biosynthesized 68.31 ± 2.15 mg/l of Zn-CP III. Finally, fed-batch fermentation allowed for the production of 132.09 mg/l of Zn-CP III. This titer represents the highest in bacterial production of Zn-CP III reported to date, to our knowledge. This study demonstrates that engineered C. glutamicum can be a robust biotechnological model for the production of photosensitizer Zn-porphyrin.

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Improved catalytic activities of a dye-decolorizing peroxidase (DyP) by overexpression of ALA and heme biosynthesis genes in Escherichia coli

Cited by 19 publications

References 45 publications

Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

High overexpression of dye decolorizing peroxidase TfuDyP leads to the incorporation of heme precursor protoporphyrin IX

Biosynthesis of organic photosensitizer Zn-porphyrin by diphtheria toxin repressor (DtxR)-mediated global upregulation of engineered heme biosynthesis pathway in Corynebacterium glutamicum

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