ArticleMicrobial cell factories2020
Improved thermostability of creatinase from Alcaligenes Faecalis through non-biased phylogenetic consensus-guided mutagenesis.
Article in Microbial cell factories, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 18 citations in OpenAlex.
- Investigation of regioselectivity and thermostability of free and immobilized Pleurotus citrinopileatus lipase.Applied microbiology and biotechnology · 2026Article
- Optimizing enzyme thermostability by combining multiple mutations using protein language model.mLife · 2024Article
- Thermostability enhancement and insight of L-asparaginase from Mycobacterium sp. via consensus-guided engineering.Applied microbiology and biotechnology · 2023Article
- Simultaneously improving the specific activity and thermostability of α-amylase BLA by rational design.Bioprocess and biosystems engineering · 2022Article
- A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens.AMB Express · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundEnzymatic quantification of creatinine has become an essential method for clinical evaluation of renal function. Although creatinase (CR) is frequently used for this purpose, its poor thermostability severely limits industrial applications. Herein, we report a novel creatinase from Alcaligenes faecalis (afCR) with higher catalytic activity and lower K
resultsWe applied a non-biased phylogenetic consensus method to identify 59 candidate consensus residues from 24 creatinase family homologs for screening afCR mutants with improved thermostability. Twenty-one amino acids of afCR were selected to mutagenesis and 11 of them exhibited improved thermostability compared to the parent enzyme (afCR-M0). Combination of single-site mutations in sequential screens resulted in a quadruple mutant D17V/T199S/L6P/T251C (M4-2) which showed ~ 1700-fold enhanced half-life at 57 °C and a 4.2 °C higher T
conclusionsResults of this study clearly demonstrated that the non-biased-phylogenetic consensus design for improvement of thermostability in afCR is effective and promising in improving the thermostability of more enzymes.
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