Effect of attaching hydrophilic oligopeptides to the C-terminus of organic solvent-tolerant metal-free bromoperoxidase BPO-A1 from Streptomyces aureofaciens on organic solvent-stability.

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2022
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Abstract
Metal-free bromoperoxidase BPO-A1 from Streptomyces aureofacience was selected among several similar enzymes exhibiting brominating activity as the most stable haloperoxidase against 70%(v/v) methanol. A comparison of the BPO-A1 and octahistidine-tagged BPO-A1 at the C-terminus (BPO-A1-His) revealed that the His-tag enhanced the organic solvent-stability of BPO-A1 with pH- and heat-stabilities. Additionally, the contribution of the hydrophilicity at the C-terminal of BPO-A1 to the organic solvent-stability was confirmed employing several mutants bearing hydrophilic oligopeptides. Fortunately, two excellent mutants, BPO-A1-Lys and BPO-A1-Arg, with high stabilities against various water-miscible organic solvents were obtained. In conclusion, the enhancing effect of the hydrophilic oligopeptides on the organic solvent-stability was associated with a decrease in the hydrophobic surface area near the C-terminus.
Reference Key
china2022effectbiochemical Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors China, Hideyasu;Ogino, Hiroyasu;
Journal Biochemical and biophysical research communications
Year 2022
DOI
10.1016/j.bbrc.2022.12.012
URL
Keywords
bpo-a1 dimer formation his-tag hydrophilic oligopeptides hydrophobic core metal-free bromoperoxidase organic solvent-stability

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