Degradation of the phenolic β-ether lignin model dimer and dyes by dye-decolorizing peroxidase from Bacillus amyloliquefaciens.

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.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Yang J,Gao T,Zhang Y,Wang S,Li H,Li S,Wang S

doi

10.1007/s10529-019-02696-0

subject

Has Abstract

pub_date

2019-09-01 00:00:00

pages

1015-1021

issue

8-9

eissn

0141-5492

issn

1573-6776

pii

10.1007/s10529-019-02696-0

journal_volume

41

pub_type

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