Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1

Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae alpha-amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared wi...

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Bibliographic Details
Published in:Applied and environmental microbiology 2000-04, Vol.66 (4), p.1754-1758
Main Authors: SUGANO, Y, NAKANO, R, SASAKI, K, SHODA, M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amyB promoter
Aspergillus oryzae
Aspergillus oryzae - enzymology
Aspergillus oryzae - genetics
Bacteria
Biological and medical sciences
Biotechnology
Coloring Agents - metabolism
Culture Media
Dyes
dyp gene
DyP protein
Enzyme engineering
Fermentation
Fundamental and applied biological sciences. Psychology
Geotrichum - enzymology
Geotrichum - genetics
Geotrichum candidum
Hydrogen-Ion Concentration
Methods. Procedures. Technologies
Microbiology
Molecular Sequence Data
Peroxidases - chemistry
Peroxidases - genetics
Peroxidases - isolation & purification
Peroxidases - metabolism
Physiology and Biotechnology
Plasmids
Polymerase Chain Reaction
Production of selected enzymes
rDyP protein
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Sequence Analysis, Protein
Substrate Specificity
Temperature
Transformation, Genetic
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Summary:Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae alpha-amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared with that of the purified native DyP from Dec 1. No exogenous heme was necessary for the expression of rDyP in A. oryzae. From the N-terminal amino acid sequence analyses of native DyP and rDyP, the absence of a histidine residue in both DyPs, which was considered to be important for heme binding of DyP, was confirmed. These results suggest that rDyP without a typical heme-binding region produced by A. oryzae exhibits a function similar to that of native DyP.
ISSN:0099-2240
1098-5336
DOI:10.1128/AEM.66.4.1754-1758.2000