Production, purification, and characterization of a novel cold-active superoxide dismutase from the Antarctic strain Aspergillus glaucus 363.

The Antarctic fungal strain Aspergillus glaucus 363 produces cold-active (CA) Cu/Zn-superoxide dismutase (SOD). The strain contains at least one gene encoding Cu/Zn-SOD that exhibited high homology with the corresponding gene of other Aspergillus species. To our knowledge, this is the first nucleotide sequence of a CA Cu/Zn-SOD gene in fungi.

Biodegradation of phenol by Antarctic strains of Aspergillus fumigatus.

Taxonomic identification of three newly isolated Antarctic fungal strains by their 18S rDNA sequences revealed their affiliation with Aspergillus fumigatus. Phenol (0.5 g/l) as the sole carbon source was completely degraded by all strains within less than two weeks.

Influence of phenolic substrates utilised by yeast on the degradation kinetics.

The degradation kinetics of different phenolic substrates utilised by R57 was studied. The following compounds were used as substrates: , resorcinol, hydroquinone, 3-nitrophenol, 2,6-dinitrophenol, 3-chloro phenol and -cresol. The specific degradation rates ( ) were described by a Haldane kinetic model.

Cresols utilization by Trametes versicolor and substrate interactions in the mixture with phenol.

The ability of the white rot fungus Trametes versicolor strain 1 to degrade and utilize methylated phenols (cresols) was established for the first time in a medium not containing any other carbon components. The data obtained demonstrated the better potential of the strain to assimilate p-cresol instead of o- or m- cresol. The 0.

Molecular analysis of phenol-degrading microbial strains.

In an attempt to estimate the occurrence of phenol hydroxylase-related gene sequences we performed a dot blot hybridization assay with DNA from phenol utilizing Trichosporon cutaneum R57 strain NBIMCC 2414 and microbial isolates from different wastewaters. The used oligonucletides were homologous to the 5'-end of TORPHD locus (NCBI)-coding phenol hydroxylase in Trichosporon cutaneum ATCC 46490 and to the 5'-end of TORCCMLE locus (NCBI)-coding cis,cis-muconate-lactonizing enzyme in Trichosporon cutaneum ATCC 58094. Two microbial strains, Escherichia coli JM 109 and Lactobacillus acidophilus ATCC 4356, incapable to degrade phenol were used as negative controls.

Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain.

The phenol-degrading strain Trichosporon cutaneum R57 utilizes various aromatic and aliphatic compounds as a sole carbon and energy source. The intracellular activities of phenol hydroxylase [EC 1.14.

Selection and characterization of L-ethionine resistant mutants of Trichosporon cutaneum.

Trichosporon cutaneum R57 and its L-ethionine resistant mutant NZ94 strain were investigated. The amino acid analyses of cell content of both strains were carried out. The pool of free methionine in the mutant strain is enhanced 16.