ArticleWorld journal of microbiology & biotechnology2019
Lys-Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions.
Article in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed, 16 citations in OpenAlex.
- Thermostable Proteases fromMicroorganisms · 2025Review
- Enzymes for production of whey protein hydrolysates and other value-added products.Applied microbiology and biotechnology · 2024Review
- Computational design of newly engineered DARPins as HER2 receptor inhibitors for breast cancer treatment.Research in pharmaceutical sciences · 2023Article
- Improving the Specific Activity and Thermostability of Psychrophilic Xylosidase AX543 by Comparative Mutagenesis.Foods (Basel, Switzerland) · 2022Article
- Article
- Rational design of a new variant of Reteplase with optimized physicochemical profile and large-scale production in Escherichia coli.World journal of microbiology & biotechnology · 2022Article
- Biochemical Characterization and Structural Insight into Interaction and Conformation Mechanisms ofMolecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Neutral proteases have broad application as additives in modern laundry detergents and therefore, thermostability is an integral parameter for effective production of protein crystals. To improve thermostability, the contribution of individual residues of Bacillus cereus neutral protease was examined by site-directed mutagenesis. The Lys11Arg and Lys211Arg mutants clearly possessed improved thermostabilities (T
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Registered trials
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