ArticleNature communications2025
An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Eutectozymes as Soft Hybrid Materials for Advanced Biocatalysis.Advanced materials (Deerfield Beach, Fla.) · 2026Article
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- Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Metallothionein-Inspired Asymmetric Heteroatom Doping of Single-Atom Nanozymes for Multi-Enzyme Biocatalysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Function and Engineering of a Food Enzyme Under Coupled High-Temperature-Pressure Conditions: Insights from Molecular Dynamics Simulation and Experimental Validation.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
11 authors.
Funding
Abstract
Lipase represents one of the most important industrial biocatalysts, with a global market value of $590.5 million by 2020. However, their catalytic efficiency is often hindered by a closed "lid" conformation. Here, we present an aggregation-induced conformation locking strategy that enables the facile synthesis of highly activated lipase hybrid biocatalysts. Lipase is self-activated into an open-lid conformation via solvent-mediated aggregation, followed by conformational locking within a two-dimensional metal-organic framework (MOF). The resulting MOF biocatalyst provides high accessibility to the locked lipase aggregates through its long-range ordered pore channels, achieving a hydrolytic efficiency 5.30 times greater than that of native lipase. To the best of our knowledge, this represents a record-high activation efficiency for ester hydrolysis among the reported lipase-based hybrid biocatalysts to date. We also demonstrate its feasibility to catalytically accelerate transesterification and esterification reactions, showing up to as 6.64 times higher yield than native lipase and impressive recyclability.
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