ArticleMolecular biotechnology2019
Production of Galactose Oxidase Inside the Fusarium fujikuroi Species Complex and Recombinant Expression and Characterization of the Galactose Oxidase GaoA Protein from Fusarium subglutinans.
Article in Molecular biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Fusarium Genome Sequencing and Assembly.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Expansion of Auxiliary Activity Family 5 sequence space via biochemical characterization of six new copper radical oxidases.Applied and environmental microbiology · 2024Article
- Characterization of a Galactose Oxidase fromFoods (Basel, Switzerland) · 2023Article
- Copper-radical oxidases: A diverse group of biocatalysts with distinct properties and a broad range of biotechnological applications.Engineering microbiology · 2022Review
- A survey of substrate specificity among Auxiliary Activity Family 5 copper radical oxidases.Cellular and molecular life sciences : CMLS · 2021Article
- Two Fusarium copper radical oxidases with high activity on aryl alcohols.Biotechnology for biofuels · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Galactose oxidase catalyzes a two-electron oxidation, mainly from the C6 hydroxyl group of D-galactose, with the concomitant reduction of water to hydrogen peroxide. This enzyme is secreted by Fusarium species and has several biotechnological applications. In this study, a screening of galactose oxidase production among species of the Fusarium fujikuroi species complex demonstrated Fusarium subglutinans to be the main producer. The truncated F. subglutinans gaoA gene coding for the mature galactose oxidase was expressed from the prokaryotic vector pTrcHis2B in the E. coli Rosetta™ (DE3) strain. The purified recombinant enzyme presented temperature and pH optima of 30 °C and 7.0, respectively, K
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