ArticleJournal of industrial microbiology & biotechnology2014
Directed evolution of GH43 β-xylosidase XylBH43 thermal stability and L186 saturation mutagenesis.
Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Development of Therapeutic Chimeric Uricase by Exon Replacement/Restoration and Site-Directed Mutagenesis.International journal of molecular sciences · 2016Article
- Highly thermostable GH39 β-xylosidase from a Geobacillus sp. strain WSUCF1.BMC biotechnology · 2014Article
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Authors and funding
8 authors at 4 institutions in 1 country.
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Abstract
Directed evolution of β-xylosidase XylBH43 using a single round of gene shuffling identified three mutations, R45K, M69P, and L186Y, that affect thermal stability parameter K(t)⁰·⁵ by -1.8 ± 0.1, 1.7 ± 0.3, and 3.2 ± 0.4 °C, respectively. In addition, a cluster of four mutations near hairpin loop-D83 improved K(t)⁰·⁵ by ~3 °C; none of the individual amino acid changes measurably affect K(t)⁰·⁵. Saturation mutagenesis of L186 identified the variant L186K as having the most improved K(t)⁰·⁵ value, by 8.1 ± 0.3 °C. The L186Y mutation was found to be additive, resulting in K(t)⁰·⁵ increasing by up to 8.8 ± 0.3 °C when several beneficial mutations were combined. While k cat of xylobiose and 4-nitrophenyl-β-D-xylopyranoside were found to be depressed from 8 to 83 % in the thermally improved mutants, K(m), K(ss) (substrate inhibition), and K(i) (product inhibition) values generally increased, resulting in lessened substrate and xylose inhibition.
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