ArticleProtein science : a publication of the Protein Society2026
A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.Protein science : a publication of the Protein Society · 2026Article
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6 authors.
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Abstract
Laccases are versatile, multicopper oxidases with broad biotechnological applications due to their ability to oxidize a wide range of substrates. Here, we introduce a computational pipeline that combines sequence filtering, Monte Carlo simulations, and quantum mechanical spin density calculations to identify laccase candidates tailored to specific substrates from large databases. Using methyl syringate as a proof of concept, we selected 37 laccase sequences for heterologous expression in Aspergillus oryzae. Of these, 21 were produced in soluble form, and 7 showed significant activity. Further kinetic and biochemical analysis identified two candidates, KAI0175247.1 and EPT01171.1, that outperformed a commercial Myceliophthora thermophila laccase (Mtl) in catalytic activity, while also displaying comparable or higher optimal temperatures. At 30°C, KAI0175247.1 and EPT01171.1 exhibited approximately 2.7- and 1.8-fold higher k
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