The effect of mutations near the T1 copper site on the biochemical characteristics of the small laccase from Streptomyces coelicolor A3(2)

Prins, Alaric; Kleinsmidt, L.; Khan, Nuraan; Kirby, Bronwyn M.; Kudanga, Tukayi; Vollmer, J.; Pleiss, Jürgen; Burton, Stephanie G.; Roes‐Hill, Marilize Le

doi:10.1016/j.enzmictec.2014.10.003

Cited by 44 publications

(29 citation statements)

References 48 publications

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“…In the environment, these enzymes play a role in the degradation of complex polymers (lignin, humic acid), lignification, detoxification, pathogenicity, morphogenesis, sporulation, polymerization of melanin and spore coat, while they have found application in the field of biotechnology, bioremediation, food processing, medicine, pharmacy, and the textile, pulp, and paper industry . Previously isolated laccases from Streptomyces strains together with lignin peroxidases were shown to be involved in lignin degradation.…”

Section: Discussionmentioning

confidence: 99%

Biocatalytic potential of Streptomyces spp. isolates from rhizosphere of plants and mycorrhizosphere of fungi

Spasic

Mandic

Radivojević

et al. 2018

Biotech and App Biochem

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Biocatalytic potential of Streptomyces strains isolated from the rhizosphere of plants and from mycorrhizosphere of fungi has been investigated. A total of 118 Streptomyces isolates were selected and functionally screened for 10 different biotechnologically important enzymatic activities: hydrolase (cellulase, cutinase, gelatinase, lipase, protease, polyhydroxyalkanoate (PHA) depolymerase), phenol oxidase and peroxidase (laccase, tyrosinase, and lignin peroxidase), and aminotransferase. Out of 118 tested Streptomyces spp., 90% showed at least one enzymatic activity. The most abundant were enzymes involved in the biomass degradation, as the production of cutinase, cellulase, and lignin peroxidase were detected in 31%, 40%, and 48% of the isolates, respectively. The improved specific activities of lipase (isolates BV315 and BV100) and tyrosinase (isolates BV87 and BV88) were shown in comparison with the industrially relevant activities of Pseudomonas strains. Plant rhizosphere soils were more prolific source of Streptomyces strains with biocatalytic potential in comparison with mycorrhizosphere soils. Overall, 284 enzyme activities among 118 Streptomyces isolates have been detected. This is the first comprehensive screening of Streptomyces isolates from rhizosphere and mycorrhizosphere soils for novel biocatalysts, showing that specific environmental habitats, such as rhizosphere soils, are "treasure troves" of Streptomyces with biocatalytic potential.

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Section: Discussionmentioning

confidence: 99%

Biocatalytic potential of Streptomyces spp. isolates from rhizosphere of plants and mycorrhizosphere of fungi

Spasic

Mandic

Radivojević

et al. 2018

Biotech and App Biochem

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“…In this study, we identified CueO mutants at another position (G276) with high activity; in particular, the G276R mutant exhibited greater activity than the wild-type protein. Structural analyses revealed that the G276 residue is located near the active site of the enzyme and close to the methionine-rich helix (residues 329-343) (Prins et al 2015;Roberts et al 2002) (Fig. 6).…”

Section: Kinetic Parametersmentioning

confidence: 99%

“…There are lots of substrates for the laccase. If the laccase could oxidize the substrate ABTS with high efficiency, the laccase usually has the good catalytic efficiency to other substrates (Camarero et al 2012;Prins et al 2015). In the The kinetic parameters were measured under optimal temperatures and pHs of CueO,G276R,G276K,G276Y,and G276N (70,60,30,50, and 50 °C and 3.5, 3.5, 2.5, 2.5, and 2.5, respectively).…”

Section: Oxidation Of Benzo[α]pyrene By Cueo and Its Mutantsmentioning

confidence: 99%

Identification of bacterial laccase cueO mutation from the metagenome of chemical plant sludge

Yue

Yang

Zhao

et al. 2017

Bioresour. Bioprocess.

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Background:The metagenome contains plenty of genetic resources and can be used to search for the novel gene or mutant. Results:In this study, the bacterial laccase gene (cueO) with single or multiple mutations was directly cloned based on the metagenome of a chemical plant sludge. An interesting mutation (G276R) was identified from those cloned mutants. The other mutants (G276N, G276Y, and G276K) with improved catalytic efficiency were identified by the saturation mutagenesis on residue G276. The optimal temperature for wild-type CueO enzyme activity was about 70 °C, compared to 60 °C, 50 °C, 50 °C, and 30 °C for the G276R, G276N, G276Y, and G276K mutant enzymes, respectively. The catalytic efficiency (k cat /K m ) with 8 mmol Cu 2+ of the G276R, G276N, G276Y, and G276K mutants was 1.2-, 2.7-, 1.3-, and 2.7-fold, respectively, compared to the wild-type enzyme. In addition, the mutants G276R, G276N, G276Y, and G276K oxidized the carcinogen benzo[α]pyrene more efficiently compared to the wild-type enzyme. Conclusion:All of the results indicate that G276 of CueO plays an important role in enzyme activity, and the useful mutants can be identified based on the metagenome.

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“…The purified laccase can be gently induced by a low concentration of organic solvent (5% methanol and ethanol), which is consistent with the recombinant laccase from B. licheniformis [Lu et al, 2013]. However, like most laccases from fungi and bacteria, it was significantly decreased by some inhibitors, such as SDS, L -cysteine, and EDTA, which may affect the type I copper binding site of laccase by chelating with Cu 2+ [Johannes and Majcherczyk, 2000;Prins et al, 2015].…”

Section: Discussionmentioning

confidence: 64%

Overexpression of a Laccase with Dye Decolorization Activity from Bacillus sp. Induced in Escherichia coli

Guo

Zheng²,

Jiang³

et al. 2017

Microb Physiol

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Laccases from bacteria have been widely studied in the past 2 decades due to the higher growth rate of bacteria and their excellent thermal and alkaline pH stability. In this study, a novel laccase gene was cloned from Bacillus sp., analyzed, and functionally expressed in Escherichia coli. The laccase was highly induced in the E. coli expression system with a maximum intracellular activity of 16 U mg^-1 protein. The optimal temperature and pH of the purified laccase were 40°C and 4.6, respectively, when ABTS (2,2'-azino-bis[3-ethylbenzothiazoline-6-sulfonate]) was used as the substrate. The purified laccase showed high stability in the pH range of 3.0-9.0, and retained more than 70% of its activity after 24 h of incubation at 40°C with a pH value of 9.0. Furthermore, the enzyme exhibited extremely high temperature and ion metal tolerance. The half-life of the purified laccase at 70°C was 15.9 h. The purified laccase could efficiently decolorize 3 chemical dyes, especially in the presence of ABTS as a mediator. The high production of this laccase in E. coli and exceptional characteristics of the recombinant enzyme protein make it a promising candidate for industrial applications.

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The effect of mutations near the T1 copper site on the biochemical characteristics of the small laccase from Streptomyces coelicolor A3(2)

Cited by 44 publications

References 48 publications

Biocatalytic potential of Streptomyces spp. isolates from rhizosphere of plants and mycorrhizosphere of fungi

Biocatalytic potential of Streptomyces spp. isolates from rhizosphere of plants and mycorrhizosphere of fungi

Identification of bacterial laccase cueO mutation from the metagenome of chemical plant sludge

Overexpression of a Laccase with Dye Decolorization Activity from <b><i>Bacillus</i></b> sp. Induced in <b><i>Escherichia coli</i></b>

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