ArticleInternational journal of biological macromolecules2019
Simulation-guided enzyme discovery: A new microbial source of cellobiose 2-epimerase.
Article in International journal of biological macromolecules, 2019. 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, 40 citations in OpenAlex.
- Characterization of novel cellobiose 2-epimerases from Teredinibacter Haidensis and Cellvibrio Japonicus.BMC biotechnology · 2026Article
- Improved biosynthesis of lactulose by a novel thermostable cellobiose-2-epimerase generated through semi-rational mutagenesis.World journal of microbiology & biotechnology · 2025Article
- Identification of a novel cellobiose 2-epimerase fromFrontiers in microbiology · 2025Article
- Computer-aided design of novel cellobiose 2-epimerase for efficient synthesis of lactulose using lactose.Bioprocess and biosystems engineering · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Cellobiose 2-epimerase (CE) is a promising industrial enzyme that can be utilized in the dairy industry. More thermostable CEs from different microorganisms are still needed for a higher lactulose productivity. This study demonstrated the feasibility to use molecular dynamics (MD) simulation as the preliminary computational filter for thermostable enzymes screening. Sequence information of eleven uncharacterized CEs were chosen to be analyzed by MD simulations. The CE from Dictyoglomus thermophilum (Dith-CE) was determined experimentally to be one of the most thermostable CEs with the highest epimerization (160 ± 6.5 U mg
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