Aspergillus nidulans

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Bingui Wang - One of the best experts on this subject based on the ideXlab platform.

Liliane Fraga Costa Ribeiro - One of the best experts on this subject based on the ideXlab platform.

  • a novel thermostable xylanase gh10 from malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology
    Biotechnology for Biofuels, 2014
    Co-Authors: Liliane Fraga Costa Ribeiro, Rosymar Coutinho De Lucas, Gabriela Leal Vitcosque, Richard J Ward, Marcelo Ventura Rubio, Andre Damasio, Fabio M Squina, Rebecca C Gregory, Paul H Walton
    Abstract:

    The search for novel thermostable xylanases for industrial use has intensified in recent years, and thermophilic fungi are a promising source of useful enzymes. The present work reports the heterologous expression and biochemical characterization of a novel thermostable xylanase (GH10) from the thermophilic fungus Malbranchea pulchella, the influence of glycosylation on its stability, and a potential application in sugarcane bagasse hydrolysis. Xylanase MpXyn10A was overexpressed in Aspergillus nidulans and was active against birchwood xylan, presenting an optimum activity at pH 5.8 and 80°C. MpXyn10A was 16% glycosylated and thermostable, preserving 85% activity after 24 hours at 65°C, and deglycosylation did not affect thermostability. Circular dichroism confirmed the high alpha-helical content consistent with the canonical GH10 family (β/α)8 barrel fold observed in molecular modeling. Primary structure analysis revealed the existence of eight cysteine residues which could be involved in four disulfide bonds, and this could explain the high thermostability of this enzyme even in the deglycosylated form. MpXyn10A showed promising results in biomass degradation, increasing the amount of reducing sugars in bagasse in natura and in three pretreated sugarcane bagasses. MpXyn10A was successfully secreted in Aspergillus nidulans, and a potential use for sugarcane bagasse biomass degradation was demonstrated.

Minghui Wang - One of the best experts on this subject based on the ideXlab platform.

Paul H Walton - One of the best experts on this subject based on the ideXlab platform.

  • a novel thermostable xylanase gh10 from malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology
    Biotechnology for Biofuels, 2014
    Co-Authors: Liliane Fraga Costa Ribeiro, Rosymar Coutinho De Lucas, Gabriela Leal Vitcosque, Richard J Ward, Marcelo Ventura Rubio, Andre Damasio, Fabio M Squina, Rebecca C Gregory, Paul H Walton
    Abstract:

    The search for novel thermostable xylanases for industrial use has intensified in recent years, and thermophilic fungi are a promising source of useful enzymes. The present work reports the heterologous expression and biochemical characterization of a novel thermostable xylanase (GH10) from the thermophilic fungus Malbranchea pulchella, the influence of glycosylation on its stability, and a potential application in sugarcane bagasse hydrolysis. Xylanase MpXyn10A was overexpressed in Aspergillus nidulans and was active against birchwood xylan, presenting an optimum activity at pH 5.8 and 80°C. MpXyn10A was 16% glycosylated and thermostable, preserving 85% activity after 24 hours at 65°C, and deglycosylation did not affect thermostability. Circular dichroism confirmed the high alpha-helical content consistent with the canonical GH10 family (β/α)8 barrel fold observed in molecular modeling. Primary structure analysis revealed the existence of eight cysteine residues which could be involved in four disulfide bonds, and this could explain the high thermostability of this enzyme even in the deglycosylated form. MpXyn10A showed promising results in biomass degradation, increasing the amount of reducing sugars in bagasse in natura and in three pretreated sugarcane bagasses. MpXyn10A was successfully secreted in Aspergillus nidulans, and a potential use for sugarcane bagasse biomass degradation was demonstrated.

Michelle Momany - One of the best experts on this subject based on the ideXlab platform.

  • Internuclear diffusion of histone H1 within cellular compartments of Aspergillus nidulans
    2018
    Co-Authors: Alexander P. Mela, Michelle Momany
    Abstract:

    Histone H1 is an evolutionarily conserved linker histone protein that functions in arranging and stabilizing chromatin structure and is frequently fused to a fluorescent protein to track nuclei in live cells. In time-lapse analyses, we observed stochastic exchange of photoactivated Dendra2-histone H1 protein between nuclei within the same cellular compartment. We also observed exchange of histones between genetically distinct nuclei in a heterokaryon derived from fusion of strains carrying histone H1-RFP or H1-GFP. Subsequent analysis of the resulting uninucleate conidia containing both RFP- and GFP-labeled histone H1 proteins showed only parental genotypes, ruling out genetic recombination and diploidization. These data together suggest that the linker histone H1 protein can diffuse between non-daughter nuclei in the filamentous fungus Aspergillus nidulans.

  • analysis of cell wall sugars in the pathogen Aspergillus fumigatus and the saprophyte Aspergillus nidulans
    Mycologia, 2000
    Co-Authors: Gretel M Guest, Michelle Momany
    Abstract:

    Sugars from cell walls of Aspergillus fumi- gatus and Aspergillus nidulans were analyzed by gas chromatography/mass spectroscopy. The walls of both fungi contain similar levels of glucose, galactose, and mannose. A. fumigatus walls contain 50% less N- acetylglucosamine than A. nidulans walls. In addi- tion, N-acetylgalactosamine is present at low levels in the walls of A. fumigatus and absent in the walls of A. nidulans.