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• W2025849287 abstract "Biotechnology applications of horseradish peroxidase (HRP) would benefit from access to tailor-made variants with greater specific activity, lower Km for peroxide, and higher thermostability. Starting with a mutant that is functionally expressed in Saccharomyces cerevisiae, we used random mutagenesis, recombination, and screening to identify HRP-C mutants that are more active and stable to incubation in hydrogen peroxide at 50°C. A single mutation (N175S) in the HRP active site was found to improve thermal stability. Introducing this mutation into an HRP variant evolved for higher activity yielded HRP 13A7-N175S, whose half-life at 60°C and pH 7.0 is three times that of wild-type (recombinant) HRP and a commercially available HRP preparation from Sigma (St. Louis, MO). The variant is also more stable in the presence of H2O2, SDS, salts (NaCl and urea), and at different pH values. Furthermore, this variant is more active towards a variety of small organic substrates frequently used in diagnostic applications. Site-directed mutagenesis to replace each of the four methionine residues in HRP (M83, M181, M281, M284) with isoleucine revealed no mutation that significantly increased the enzyme's stability to hydrogen peroxide. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 76: 99–107, 2001." @default.
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• W2025849287 date "2001-01-01" @default.
• W2025849287 modified "2023-09-23" @default.
• W2025849287 title "Functional expression and stabilization of horseradish peroxidase by directed evolution inSaccharomyces cerevisiae" @default.
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• W2025849287 doi "https://doi.org/10.1002/bit.1149" @default.
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