ArticleMolecular and cellular biochemistry2018
Point mutation Arg153-His at surface of Bacillus lipase contributing towards increased thermostability and ester synthesis: insight into molecular network.
Article in Molecular and cellular biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed, 13 citations in OpenAlex.
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases.Biotechnology for biofuels · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
In order to design proteins with improved properties i.e. thermostability, catalytic efficiency and to understand the mechanisms underlying, a thermostable variant of Bacillus lipase was generated by site-directed mutagenesis with enhanced thermal (∆Tm = + 12 °C) and chemical (∆Cm denaturation for Gdmcl = + 1.75 M) stability as compared to WT. Arg153-His variant showed 72-fold increase in thermostability (t
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Registered trials
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