Abstract
Objective
The dye-decolorizing peroxidase from Bacillus amyloliquefaciens, BaDyP, was identified to be an efficient catalyst for the degradation of phenolic β-ether lignin model dimer guaiacylglycerol-β-guaiacyl ether (GGE) and dyes.
Results
Efeb gene encoding BaDyP from B. amyloliquefaciens MN-13 consisted of 1257 bp and the open reading frame encoded 418 amino acids. The efeb gene was expressed in Escherichia coli BL21 and a recombinant BaDyP of 50 kDa was achieved. The BaDyP exhibited activity in oxidizing GGE and decolorizing azo and triphenylmethane dyes. At pH 4.5 and 30 °C the BaDyP not only completely degraded GGE by the cleavage of β-O-4 ether bond and Cα–Cβ bond, and Cα oxidation without any oxidative mediator, but also decolorized four synthetic dyes, including congo red, bromine cresol green, eriochrome black T and crystal violet. This was achieved with decolorization rates of 65.7%, 70.62%, 80.06% and 62.09%, respectively, after 72 h of incubation.
Conclusions
BaDyP was identified as a bacteria peroxidase with great potential for the degradation of lignin and bioremediation of dye-contamination.
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Acknowledgements
This work was sponsored by the Hebei Science and Technology Support Program (1222605).
Supporting Information
Supplementary Figure 1—Identification of GGE-degradation products by comparison of mass spectra in NIST.
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Yang, J., Gao, T., Zhang, Y. et al. Degradation of the phenolic β-ether lignin model dimer and dyes by dye-decolorizing peroxidase from Bacillus amyloliquefaciens. Biotechnol Lett 41, 1015–1021 (2019). https://doi.org/10.1007/s10529-019-02696-0
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DOI: https://doi.org/10.1007/s10529-019-02696-0