Evidence map›Paper›PMID 42133171›Full record

ArticleApplied biochemistry and biotechnology2026

Extraction, Purification, and Biochemical Characterization of Tyrosinase from Agaricus bisporus: An Important Enzyme in Biotechnology Applications.

Mohammed Harir, Hamdi Bendif, Mohammed El-Shazly, Nadhem Aissani, Soulef Dib, Susana Rodríguez-Couto, Fehmi Boufahja, Stefania Garzoli

Abstract read
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Article in Applied biochemistry and biotechnology, 2026. 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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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Mohammed HarirBiology of Microorganisms and Biotechnology Laboratory, University of Oran 1, Ahmed Ben Bella, BP1524, Oran El Mnaouer, Oran, 31000, Algeria.
Hamdi BendifBiology Department, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, 11623, Saudi Arabia.
Mohammed El-ShazlyDepartment of Pharmacognosy, Faculty of Pharmacy, Ain-Shams University, Cairo, 11566, Egypt.
Nadhem AissaniLaboratoire de Physiologie Fonctionnelle Et Valorisation Des Bio-Resssources, Institut Supérieur de Biotechnologie de Béja, Université de Jendouba, Avenue Habib Bourguiba, B.P, 382-9000, Béja, Tunisie.
Soulef DibBiology of Microorganisms and Biotechnology Laboratory, University of Oran 1, Ahmed Ben Bella, BP1524, Oran El Mnaouer, Oran, 31000, Algeria.
Susana Rodríguez-CoutoDepartment of Separation Science, LUT School of Engineering Science, LUT University, Sammonkatu 12, Mikkeli, 50130, Finland.
Fehmi BoufahjaBiology Department, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, 11623, Saudi Arabia.
Stefania GarzoliDepartment of Chemistry and Technologies of Drug, Sapienza University, Rome, 00185, Italy. stefania.garzoli@uniroma1.it.ORCID http://orcid.org/0000-0001-8535-0533

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosinase, a copper-containing enzyme with broad biological and industrial applications, occurs widely in nature but remains underexplored in edible mushrooms such as Agaricus bisporus. This study reports the extraction, purification, and biochemical characterization of tyrosinase from A. bisporus fruiting bodies. The enzyme was purified via ammonium sulfate precipitation (60% saturation), dialysis, and Sephadex G-200 gel filtration chromatography, achieving 163 fold purification with a specific activity of 1.26 U/mg and 20% recovery. SDS-PAGE revealed a tetrameric structure with a subunit molecular mass of 128-130 kDa. Kinetic parameters were determined as Km = 0.42km = 0.42 mM for L-DOPA and Vmax = 12.5Vmax = 12.5 U/mL. The enzyme exhibited optimal activity at pH 6.5 and 50°C, with stability profiles comparable to commercial counterparts. These findings underscore the optimized purification method and the biotechnological potential of A. bisporus tyrosinase for applications in food processing, medicine, agriculture, and environmental remediation, while advancing knowledge of multicopper oxidases in fungi.

Indexed as

AgaricusBiotechnologyFungal ProteinsMonophenol MonooxygenaseElectrophoresis, Polyacrylamide GelEnzyme StabilityHydrogen-Ion ConcentrationKineticsMolecular WeightSubstrate SpecificityTemperatureFungal ProteinsMonophenol MonooxygenaseAgaricus bisporusEnzyme characterizationKineticsPurificationTyrosinase

Identifiers

PMID42133171
PMCPMC13408164

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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.