ArticleThe FEBS journal2019
nanoDSF as screening tool for enzyme libraries and biotechnology development.
Article in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 133 citations in OpenAlex.
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- Determinants of DNA Binding by Plant Homologs of 3-Methyladenine-DNA Glycosylase.Doklady. Biochemistry and biophysics · 2026Article
- Structural basis of G6P/Pi transport and inhibition in SLC37A4.Nature structural & molecular biology · 2026Article
- NbBayesLM: bayesian prediction of nanobody thermostability using protein language model.Frontiers in bioinformatics · 2026Article
- Chemical modulation of chloroplast de- and re-differentiation reveals a role for the SAL1-PAP retrograde pathway in facilitating plastid transitions.bioRxiv : the preprint server for biology · 2025Article
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- Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction.ACS chemical neuroscience · 2025Article
- Allosteric Modulation of GCase Enhances Lysosomal Activity and Reduces ER Stress in GCase-Related Disorders.International journal of molecular sciences · 2025Article
- The salty tango of brine composition and UV photochemistry effects on Halobacterium salinarum cell envelope biosignature preservation.Communications biology · 2025Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Enzymes are attractive tools for synthetic applications. To be viable for industrial use, enzymes need sufficient stability towards the desired reaction conditions such as high substrate and cosolvent concentration, non-neutral pH and elevated temperatures. Thermal stability is an attractive feature not only because it allows for protein purification by thermal treatment and higher process temperatures but also due to the associated higher stability against other destabilising factors. Therefore, high-throughput screening (HTS) methods are desirable for the identification of thermostable biocatalysts by discovery from nature or by protein engineering but current methods have low throughput and require time-demanding purification of protein samples. We found that nanoscale differential scanning fluorimetry (nanoDSF) is a valuable tool to rapidly and reliably determine melting points of native proteins. To avoid intrinsic problems posed by crude protein extracts, hypotonic extraction of overexpressed protein from bacterial host cells resulted in higher sample quality and accurate manual determination of several hundred melting temperatures per day. We have probed the use of nanoDSF for HTS of a phylogenetically diverse aldolase library to identify novel thermostable enzymes from metagenomic sources and for the rapid measurements of variants from saturation mutagenesis. The feasibility of nanoDSF for the screening of synthetic reaction conditions was proved by studies of cosolvent tolerance, which showed protein melting temperature to decrease linearly with increasing cosolvent concentration for all combinations of six enzymes and eight water-miscible cosolvents investigated, and of substrate affinity, which showed stabilisation of hexokinase by sugars in the absence of ATP cofactor. ENZYMES: Alcohol dehydrogenase (NADP
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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.