Aspergillus terreus

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Ernst H. Oliw - One of the best experts on this subject based on the ideXlab platform.

Cornelia Lass-flörl - One of the best experts on this subject based on the ideXlab platform.

  • Rep-PCR and RAPD-PCR fingerprinting of Aspergillus terreus.
    Medical mycology, 2013
    Co-Authors: Wolfgang Mutschlechner, Katharina Grif, Gerhard Blum, Cornelia Lass-flörl
    Abstract:

    We compared two PCR methods for molecular typing the medically important filamentous fungus Aspergillus terreus. In a set of 46 strains investigated we found 19 and 12 different fingerprinting types obtained by random amplified polymorphic DNA PCR (RAPD) and semi-automated repetitive element PCR (rep-PCR), respectively.

  • Potential Basis for Amphotericin B Resistance in Aspergillus terreus
    Antimicrobial agents and chemotherapy, 2008
    Co-Authors: Gerhard Blum, Susanne Perkhofer, Hubertus Haas, Markus Schrettl, Reinhard Würzner, Manfred P. Dierich, Cornelia Lass-flörl
    Abstract:

    This study investigated the basis for intrinsic amphotericin B (AMB) resistance in Aspergillus terreus. The ergosterol content, cell wall composition, and lipid peroxidation level had no influence on AMB resistance. The level of catalase production in A. terreus was significantly higher than that in A. fumigatus (P < 0.05). This higher-level production may contribute to AMB resistance in A. terreus since oxidative damage has been implicated in AMB action.

Mitsuyasu Okabe - One of the best experts on this subject based on the ideXlab platform.

  • Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1
    Journal of bioscience and bioengineering, 2002
    Co-Authors: Lies Dwiarti, Ken Yamane, Hitoshi Yamatani, Prihardi Kahar, Mitsuyasu Okabe
    Abstract:

    Abstract cis -Aconitic acid decarboxylase (CAD) was assumed to be a key enzyme in the production of itaconic acid by comparing the activity of CAD from Aspergillus terreus TN484-M1 with that of CAD from the low-itaconate yielding strain Aspergillus terreus CM85J. The constitutive CAD was purified to homogeneity from A. terreus TN484-M1 by ammonium sulfate fractionation, and column chromatography on DEAE-toyopearl, Butyl-toyopearl, and Sephacryl S200HR, and then characterized. A molecular mass of 55 kDa for the native enzyme was determined by SDS-PAGE. The enzymic activity was optimal at a pH of 6.2 and temperature of 45°C. The K m value for cis -aconitic acid was determined as 2.45 mM (pH 6.2, 37°C). The enzyme was completely inactivated by Hg + , Cu 2+ , Zn 2+ , p -chloromercuribenzoate, and 5,5′-dithio- bis (2-nitrobenzoate).

  • Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1
    Journal of bioscience and bioengineering, 2002
    Co-Authors: Lies Dwiarti, Ken Yamane, Hitoshi Yamatani, Prihardi Kahar, Mitsuyasu Okabe
    Abstract:

    cis-Aconitic acid decarboxylase (CAD) was assumed to be a key enzyme in the production of itaconic acid by comparing the activity of CAD from Aspergillus terreus TN484-M1 with that of CAD from the low-itaconate yielding strain Aspergillus terreus CM85J. The constitutive CAD was purified to homogeneity from A. terreus TN484-M1 by ammonium sulfate fractionation, and column chromatography on DEAE-toyopearl, Butyl-toyopearl, and Sephacryl S200HR, and then characterized. A molecular mass of 55 kDa for the native enzyme was determined by SDS-PAGE. The enzymic activity was optimal at a pH of 6.2 and temperature of 45 degrees C. The K(m) value for cis-aconitic acid was determined as 2.45 mM (pH 6.2, 37 degrees C). The enzyme was completely inactivated by Hg+, Cu2+, Zn2+, p-chloromercuribenzoate, and 5,5'-dithio-bis(2-nitrobenzoate).

Fredrik Jernerén - One of the best experts on this subject based on the ideXlab platform.

Stephen C. Teoh - One of the best experts on this subject based on the ideXlab platform.