ArticleMicrobial cell factories2018
Enhanced trypsin thermostability in Pichia pastoris through truncating the flexible region.
Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A Practical Guide to Computational Tools for Engineering Biocatalytic Properties.International journal of molecular sciences · 2025Review
- Unraveling the Effects of Hexametaphosphate: Insights into Trypsin Aggregation and Structural Reversal.ACS omega · 2024Article
- Enhancement of the Thermostability ofMolecules (Basel, Switzerland) · 2024Article
- Improvement of the stability and catalytic efficiency of heparan sulfate N-sulfotransferase for preparing N-sulfated heparosan.Journal of industrial microbiology & biotechnology · 2023Article
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Authors and funding
6 authors.
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Abstract
backgroundHigh thermostability is required for trypsin to have wider industrial applications. Target mutagenesis at flexible regions has been proved to be an efficient protein engineering method to enhance the protein thermostability.
resultsThe flexible regions in porcine trypsin were predicted using the methods including molecular dynamic simulation, FlexPred, and FoldUnfold. The amino acids 78-90 was predicted to be the highly flexible region simultaneously by the three methods and hence selected to be the mutation target. We constructed five variants (D3, D5, D7, D9, and D11) by truncating the region. And the variant D9 showed higher thermostability, with a 5 °C increase in T
conclusionsThese results showed that the thermostability of variant D9 was increased. The variant D9 could be expected to be a promising tool enzyme for its wider industrial applications. The method of truncating the flexible region used in our study has the potential to be used for enhancing the thermostability of other proteins.
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