ReviewAPL bioengineering2018
Review: Engineering of thermostable enzymes for industrial applications.
Review in APL bioengineering, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 2 of them syntheses that pooled it.
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
103 citing papers in PubMed, 2 syntheses or guidelines pooled it, 302 citations in OpenAlex.
- Hunt for α-amylase from metagenome and strategies to improve its thermostability: a systematic review.World journal of microbiology & biotechnology · 2022Pooled it
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Integrative machine learning approaches for enzyme kinetic parameter prediction.Briefings in bioinformatics · 2026Review
- Recent advances in AI-driven deep eutectic solvent design for biocatalysis: Co-design of extremozyme and reaction medium.Biodesign research · 2026Review
- The X-Ray Crystal Structure of BorF, the Flavin Reductase Subunit of a Two-Component Flavin-Dependent Tryptophan Halogenase.Proteins · 2026Article
- Genome-Resolved Metagenomics Reveals Thermophilic Microbial Diversity and Putative Hydrolase-Encoding Genes in the El Tatio Geothermal Field.International journal of molecular sciences · 2026Article
- Identification and Thermal Stability Modification of a Zearalenone Lactone Hydrolase ZHD30L.Toxins · 2026Article
- Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation.The FEBS journal · 2026Article
- Green biocatalysis: Box-Behnken-optimized cellulase from thermophilic Streptomyces griseorubens NBR14 for waste management and dye removal.Biodegradation · 2026Article
- Comparative Molecular Dynamics Study of the Thermal Stability of CheY Proteins from Hyperthermophilic and Mesophilic Organisms.Journal of chemical information and modeling · 2026Article
- Production of Novel Thermostable Esterases fromInternational journal of molecular sciences · 2026Article
- Medicinal chemistry meets nanotechnology: machine learning assisted colorimetric sensing platform for oxalic acid based on drug mediated copper oxide nanoparticles.RSC advances · 2026Article
- Article
- Microbial Ecology at the Nexus of Food Safety and Biotechnology With Ecological Mechanisms, Risks, and Emerging Innovations.International journal of food science · 2026Review
- Spatial fluorescence barcode by transiently luminescent DNA beads.Nature communications · 2025Article
- Cloning and Characterization of the Novel Endoglucanase Identified in Deep Subsurface Thermal Well of Biragzang (North Ossetia) by Metagenomic Analysis.Biomolecules · 2025Article
- Droplet based microfluidic and miniaturization at high-throughput level to screening heterologous secondary metabolites in microbes: A critical review.Biotechnology letters · 2025Review
- Engineering of Nocardioides acrostichi lipase: utilizing natural variation and mutational free energy to alter expression and functional properties.Journal of biological engineering · 2025Article
- Benchmarking Free Energy Calculations: Analysis of Single and Double Mutations Across Two Simulation Software Platforms for Two Protein Systems.bioRxiv : the preprint server for biology · 2025Article
- Integrated Proteomic and Molecular Identification of ThermophilicLife (Basel, Switzerland) · 2025Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic properties of some selected enzymes have long been exploited to carry out efficient and cost-effective bioconversions in a multitude of research and industrial sectors, such as food, health, cosmetics, agriculture, chemistry, energy, and others. Nonetheless, for several applications, naturally occurring enzymes are not considered to be viable options owing to their limited stability in the required working conditions. Over the years, the quest for novel enzymes with actual potential for biotechnological applications has involved various complementary approaches such as mining enzyme variants from organisms living in extreme conditions (extremophiles), mimicking evolution in the laboratory to develop more stable enzyme variants, and more recently, using rational, computer-assisted enzyme engineering strategies. In this review, we provide an overview of the most relevant enzymes that are used for industrial applications and we discuss the strategies that are adopted to enhance enzyme stability and/or activity, along with some of the most relevant achievements. In all living species, many different enzymes catalyze fundamental chemical reactions with high substrate specificity and rate enhancements. Besides specificity, enzymes also possess many other favorable properties, such as, for instance, cost-effectiveness, good stability under mild pH and temperature conditions, generally low toxicity levels, and ease of termination of activity. As efficient natural biocatalysts, enzymes provide great opportunities to carry out important chemical reactions in several research and industrial settings, ranging from food to pharmaceutical, cosmetic, agricultural, and other crucial economic sectors.
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.