Degradation of hydroxylated phenols by an Aspergillus fumigatus strain isolated from Antarctica

M. Gerginova; N. Peneva; J. Manasiev; Z. Alexieva

Degradation of hydroxylated phenols by an Aspergillus fumigatus strain isolated from Antarctica

in Industrial, medical and environmental applications of microorganisms

Autor:innen:

M. Gerginova

M. Gerginova Department of General Microbiology, Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria; zlatkama@yahoo.com

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N. Peneva

N. Peneva Department of General Microbiology, Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria; zlatkama@yahoo.com

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J. Manasiev

J. Manasiev Department of General Microbiology, Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria; zlatkama@yahoo.com

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Z. Alexieva

Z. Alexieva Department of General Microbiology, Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria; zlatkama@yahoo.com

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Art:: Kapitel

Seiten:: 93–98

DOI:: https://doi.org/10.3920/9789086867950_015

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The investigated Aspergillus fumigatus strain AL9 has been taxonomically determined by molecular methods (NCBI Acc. No. JQ 639072.1) and the ability to utilize 0.5 g/l phenol as a sole carbon source was demonstrated. It was observed that A. fumigatus strain AL9 had a different capability to degrade the isomeric forms of both hydroxylated phenols. The complete degradation and assimilation of catechol as a sole carbon source was performed for about 72 h while the hydroquinone was degraded and utilize much slower and the observed decrease of its concentrations for the same period of time was 30%. The complete hydroquinone degradation was performed in 96 h. The intracellular enzyme activities of phenol hydroxylase, catechol 1,2-dioxygenase, and hydroquinone hydroxylase in cells of A. fumigatus strain AL9, cultivated in a medium containing 0.3 g/l catechol or hydroquinone as a single carbon substrate were determined. The catechol 1,2-dioxygenase enzyme activity showed the highest activity (0.427 U/ mg protein) in the logarithmic growth phase in the case of culturing the strain in a medium sole carbon source catechol. The enzyme hydroquinone hydroxylase has kept a constant but not high level of activity (about 0.040 U/mg protein) during all phases of growth and degradation process. The gene coding for catechol 1,2-dioxygenase was identified using set of oligonucleotide primers designed in the course of this study. The DNA sequence (1,063 bp) of the catechol dioxygenase gene of the strain A. fumigatus AL9 was obtained. The BLAST analysis demonstrated 99% identity with the corresponding A. fumigatus Af293 sequence.

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Industrial, medical and environmental applications of microorganisms

Current status and trends

ISBN:: 9789086867950

Verleger:: Wageningen Academic

Print-Publikationsdatum:: 01 Nov 2014

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Degradation of hydroxylated phenols by an Aspergillus fumigatus strain isolated from Antarctica

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Industrial, medical and environmental applications of microorganisms

Current status and trends

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