ArticleApplied and environmental microbiology2014
In silico rational design and systems engineering of disulfide bridges in the catalytic domain of an alkaline α-amylase from Alkalimonas amylolytica to improve thermostability.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 51 citations in OpenAlex.
- α-Amylase: Its Structure, Molecular Modification, and Application in the Food Field.Foods (Basel, Switzerland) · 2026Review
- Open and closed structures of L-arginine oxidase by cryo-electron microscopy and X-ray crystallography.Journal of biochemistry · 2025Article
- Thermal Characterization and Interaction of the Subunits from the Multimeric Bacteriophage Endolysin PlyC.Biology · 2023Article
- Improving Both the Thermostability and Catalytic Efficiency of Phospholipase D fromInternational journal of molecular sciences · 2022Article
- Article
- Enhanced Prodigiosin Production inApplied and environmental microbiology · 2021Article
- Computational design of noncanonical amino acid-based thioether staples at N/C-terminal domains of multi-modular pullulanase for thermostabilization in enzyme catalysis.Computational and structural biotechnology journal · 2021Article
- Structure elucidation and docking analysis of 5M mutant of T1 lipase Geobacillus zalihae.PloS one · 2021Article
- Evolution of Protein Structure and Stability in Global Warming.International journal of molecular sciences · 2020Review
- Rational Design of Alginate Lyase fromMarine drugs · 2019Article
- Disulfide Bond Engineering of an Endoglucanase fromInternational journal of molecular sciences · 2019Article
- The response to selection in Glycoside Hydrolase Family 13 structures: A comparative quantitative genetics approach.PloS one · 2018Article
- Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.Scientific reports · 2017Article
- Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.Applied and environmental microbiology · 2017Article
- Elimination of a Free Cysteine by Creation of a Disulfide Bond Increases the Activity and Stability of Candida boidinii Formate Dehydrogenase.Applied and environmental microbiology · 2017Article
- Probing the role of cation-π interaction in the thermotolerance and catalytic performance of endo-polygalacturonases.Scientific reports · 2016Article
- Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration.Scientific reports · 2016Article
- Rational Design of Disulfide Bonds Increases Thermostability of a Mesophilic 1,3-1,4-β-Glucanase from Bacillus terquilensis.PloS one · 2016Article
- Engineering of isoamylase: improvement of protein stability and catalytic efficiency through semi-rational design.Journal of industrial microbiology & biotechnology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
High thermostability is required for alkaline α-amylases to maintain high catalytic activity under the harsh conditions used in textile production. In this study, we attempted to improve the thermostability of an alkaline α-amylase from Alkalimonas amylolytica through in silico rational design and systems engineering of disulfide bridges in the catalytic domain. Specifically, 7 residue pairs (P35-G426, Q107-G167, G116-Q120, A147-W160, G233-V265, A332-G370, and R436-M480) were chosen as engineering targets for disulfide bridge formation, and the respective residues were replaced with cysteines. Three single disulfide bridge mutants-P35C-G426C, G116C-Q120C, and R436C-M480C-of the 7 showed significantly enhanced thermostability. Combinational mutations were subsequently assessed, and the triple mutant P35C-G426C/G116C-Q120C/R436C-M480C showed a 6-fold increase in half-life at 60°C and a 5.2°C increase in melting temperature compared with the wild-type enzyme. Interestingly, other biochemical properties of this mutant also improved: the optimum temperature increased from 50°C to 55°C, the optimum pH shifted from 9.5 to 10.0, the stable pH range extended from 7.0 to 11.0 to 6.0 to 12.0, and the catalytic efficiency (kcat/Km) increased from 1.8 × 10(4) to 2.4 × 10(4) liters/g · min. The possible mechanism responsible for these improvements was explored through comparative analysis of the model structures of wild-type and mutant enzymes. The disulfide bridge engineering strategy used in this work may be applied to improve the thermostability of other industrial enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.