An acid-stable bacterial laccase identified from the endophyte Pantoea ananatis Sd-1 genome exhibiting lignin degradation and dye decolorization abilities
0301 basic medicine
Pantoea
Laccase
Molecular Sequence Data
Lignin
Recombinant Proteins
03 medical and health sciences
Bacterial Proteins
Amino Acid Sequence
Coloring Agents
Sequence Alignment
Genome, Bacterial
Water Pollutants, Chemical
DOI:
10.1007/s10529-015-1914-1
Publication Date:
2015-07-24T08:36:42Z
AUTHORS (12)
ABSTRACT
Isolation and identification of a novel laccase (namely Lac4) with various industrial applications potentials from an endophytical bacterium.Endophyte Sd-1 cultured in rice straw showed intra- and extra-cellular laccase activities. Genomic analysis of Sd-1 identified four putative laccases, Lac1 to Lac4. However, only Lac4 contains the complete signature sequence of laccase and shares at most 64 % sequence identity with other characterized bacterial multi-copper oxidases. Recombinant Lac4 can oxidize non-phenolic and phenolic compounds under acidic conditions and at 30-50 °C; Km values of Lac4 for ABTS at pH 2.5 and for guaiacol at pH 4.5 were 1 ± 0.15 and 6.1 ± 1.7 mM, respectively. The activity of Lac4 was stimulated by 0.8 mM Cu(2+) and 5 mM Fe(2+). In addition, Lac4 could decolorize various synthetic dyes and exhibit the degradation rate of 38 % for lignin.The data suggest that Lac4 possesses promising biotechnological potentials.
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