Tyrosinase Recovered from White Button Mushroom Waste: Extraction, Characterization, and Application in Casein Cross-Linking
Trang Thuy Tran, Zhe Xu, John Coupland, Yi Zhang

TL;DR
Researchers extracted tyrosinase from mushroom waste to use it for cross-linking proteins, offering a cost-effective way to repurpose agricultural byproducts.
Contribution
The study introduces a novel method to recover and characterize tyrosinase from white button mushroom stumps for protein modification.
Findings
Tyrosinase was successfully recovered from white button mushroom stumps and showed optimal activity at pH 7.5 and 45 °C.
Ammonium sulfate fractionation improved purification and activity recovery of the enzyme.
Partial purification and use of EDTA/PMSF enabled effective casein cross-linking despite protease interference.
Abstract
Tyrosinase catalyzes the oxidation of mono- and diphenols to o-quinones, which can polymerize and covalently cross-link proteins, but the limited availability and high cost of purified tyrosinase limit broader use. This study recovered tyrosinase from white button mushroom (Agaricus Bisporus) stumps, an underutilized byproduct, and evaluated it for food protein modification. Proteomics identified multiple tyrosinase isozymes (AbPPO3, AbPPO4, AbPPO5), and the crude tyrosinase exhibited optimal activity at pH 7.5 and 45 °C, with a prominent 43 kDa protein band. Ammonium sulfate fractionation (50–70% saturation) increased specific activity; the 50% fraction achieved 4.4-fold purification with 47% activity recovery. Effects of chemical modulators, metal ions, salts, reductants, chelators, and inhibitors were systematically assessed. Endogenous proteolysis hindered cross-linking, but partial…
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Taxonomy
Topicsmelanin and skin pigmentation · Advanced Glycation End Products research · Protein Hydrolysis and Bioactive Peptides
