ArticleInternational journal of molecular sciences2023
Enhancing the Hydrolytic Activity of a Lipase towards Larger Triglycerides through Lid Domain Engineering.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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Who cites it
5 citing papers in PubMed, 23 citations in OpenAlex.
- Quantitative Methods for Assessing True Lipase Activity Using Long-Chain Triglycerides and Complex Lipid Substrates.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Revealing the essential role of the lid in mclPHA intracellular depolymerase from Pseudomonas putida KT2440.Applied microbiology and biotechnology · 2025Article
- Review on Lipase-Catalyzed Flavor Synthesis: Global Trends and Advances.Journal of agricultural and food chemistry · 2025Review
- Insight into improved specificity and thermostability of3 Biotech · 2025Article
- Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art.Molecules (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Lipases have valuable potential for industrial use, particularly those mostly active against water-insoluble substrates, such as triglycerides composed of long-carbon chain fatty acids. However, in most cases, engineered variants often need to be constructed to achieve optimal performance for such substrates. Protein engineering techniques have been reported as strategies for improving lipase characteristics by introducing specific mutations in the cap domain of esterases or in the lid domain of lipases or through lid domain swapping. Here, we improved the lipase activity of a lipase (WP_075743487.1, or Lip
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Registered trials
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