Mareike Bongers | The University of Queensland, Australia (original) (raw)

Mareike Bongers

Address: Brisbane, Queensland, Australia

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Papers by Mareike Bongers

Research paper thumbnail of Synthetic multi-component enzyme mixtures for deconstruction of lignocellulosic biomass

Bioresource Technology, 2010

Research paper thumbnail of α-Fucosidases with different substrate specificities from two species of Fusarium

Applied Microbiology and Biotechnology, 2013

Two fungal-secreted α-fucosidases and their genes were characterized. FoFCO1 was purified from cu... more Two fungal-secreted α-fucosidases and their genes were characterized. FoFCO1 was purified from culture filtrates of Fusarium oxysporum strain 0685 grown on L-fucose and its encoding gene identified in the sequenced genome of strain 4287. FoFCO1 was active on p-nitrophenyl-α-fucoside (pNP-Fuc), but did not defucosylate a nonasaccharide (XXFG) fragment of pea xyloglucan. A putative α-fucosidase gene (FgFCO1) from Fusarium graminearum was expressed in Pichia pastoris. FgFCO1 was ~1,800 times less active on pNP-Fuc than FoFCO1, but was able to defucosylate the XXFG nonasaccharide. Although FgFCO1 and FoFCO1 both belong to Glycosyl Hydrolase family 29, they share <25 % overall amino acid identity. Alignment of all available fungal orthologs of FoFCO1 and FgFCO1 indicated that these two proteins belong to two subfamilies of fungal GH29 α-fucosidases. Fungal orthologs of subfamily 1 (to which FoFCO1 belongs) are taxonomically more widely distributed than subfamily 2 (FgFCO1), but neither was universally present in the sequenced fungal genomes. Trichoderma reesei and most species of Aspergillus lack genes for either GH29 subfamily.

Research paper thumbnail of Production of Industrially Relevant Isoprenoid Compounds in Engineered Microbes

Microbiology Monographs, 2014

Research paper thumbnail of Metabolic engineering of volatile isoprenoids in plants and microbes

Plant, Cell & Environment, 2014

Research paper thumbnail of Knock-in/Knock-out (KIKO) vectors for rapid integration of large DNA sequences, including whole metabolic pathways, onto the Escherichia coli chromosome at well-characterised loci

Microbial Cell Factories, 2013

Research paper thumbnail of Synthetic multi-component enzyme mixtures for deconstruction of lignocellulosic biomass

Bioresource Technology, 2010

Research paper thumbnail of α-Fucosidases with different substrate specificities from two species of Fusarium

Applied Microbiology and Biotechnology, 2013

Two fungal-secreted α-fucosidases and their genes were characterized. FoFCO1 was purified from cu... more Two fungal-secreted α-fucosidases and their genes were characterized. FoFCO1 was purified from culture filtrates of Fusarium oxysporum strain 0685 grown on L-fucose and its encoding gene identified in the sequenced genome of strain 4287. FoFCO1 was active on p-nitrophenyl-α-fucoside (pNP-Fuc), but did not defucosylate a nonasaccharide (XXFG) fragment of pea xyloglucan. A putative α-fucosidase gene (FgFCO1) from Fusarium graminearum was expressed in Pichia pastoris. FgFCO1 was ~1,800 times less active on pNP-Fuc than FoFCO1, but was able to defucosylate the XXFG nonasaccharide. Although FgFCO1 and FoFCO1 both belong to Glycosyl Hydrolase family 29, they share <25 % overall amino acid identity. Alignment of all available fungal orthologs of FoFCO1 and FgFCO1 indicated that these two proteins belong to two subfamilies of fungal GH29 α-fucosidases. Fungal orthologs of subfamily 1 (to which FoFCO1 belongs) are taxonomically more widely distributed than subfamily 2 (FgFCO1), but neither was universally present in the sequenced fungal genomes. Trichoderma reesei and most species of Aspergillus lack genes for either GH29 subfamily.

Research paper thumbnail of Production of Industrially Relevant Isoprenoid Compounds in Engineered Microbes

Microbiology Monographs, 2014

Research paper thumbnail of Metabolic engineering of volatile isoprenoids in plants and microbes

Plant, Cell & Environment, 2014

Research paper thumbnail of Knock-in/Knock-out (KIKO) vectors for rapid integration of large DNA sequences, including whole metabolic pathways, onto the Escherichia coli chromosome at well-characterised loci

Microbial Cell Factories, 2013

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