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ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2025

Accumulation of heavy metals in the mycelium of Abortiporus biennis and their effect on oxalate oxidase activity.

Marcin Grąz, Anna Jarosz-Wilkołazka, Jolanta Polak, Bożena Pawlikowska-Pawlęga, Justyna Kapral-Piotrowska, Wioleta Ciempiel, Marta Ruminowicz-Stefaniuk

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Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Marcin GrązDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland. marcin.graz@mail.umcs.pl.
Anna Jarosz-WilkołazkaDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Jolanta PolakDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Bożena Pawlikowska-PawlęgaDepartment of Comparative Anatomy and Anthropology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Justyna Kapral-PiotrowskaDepartment of Comparative Anatomy and Anthropology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Wioleta CiempielInstitute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290, Lublin, Poland.
Marta Ruminowicz-StefaniukDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abortiporus biennis belongs to a basidiomycete fungi with the unique ability to degrade oxalate using enzyme oxalate oxidase. Oxalate oxidase (OXO) from Abortiporus biennis is an intracellular oxalic acid-induced enzyme, which catalyses the degradation of oxalic acid to carbon dioxide and hydrogen peroxide. OXO activity was stimulated by all the heavy metals tested (copper, manganese, lead and cadmium) after addition as water-soluble salts to A. biennis fungal cultures. Manganese ions stimulated OXO activity to the greatest extent among the tested metal ions. In the presence of manganese ions, an elevated concentration of oxalate was also detected in the fungal culture after 7 days of cultivation. The manganese, lead, and cadmium ions were accumulated by the A. biennis mycelium. Among them, lead was accumulated to a great extent. It was observed that the accumulation of lead ions occurred in the vicinity of the A. biennis hyphal cell wall.

Indexed as

BasidiomycotaMetals, HeavyMyceliumOxidoreductasesCadmiumLeadManganeseOxalatesOxalic AcidCadmiumLeadManganeseMetals, Heavyoxalate oxidaseOxalatesOxalic AcidOxidoreductasesAbortiporus biennisEDXHeavy metalsOxalate oxidaseOxalic acid

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.