ArticleProtein science : a publication of the Protein Society2025
Loop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- MartiniSurf: Automated Simulations of Surface-Immobilized Biomolecular Systems with Martini.Journal of chemical information and modeling · 2026Article
- Reverse beta-oxidation for biochemical production: insights into the functional properties of key enzymes.BMB reports · 2026Review
- SegDesign: A modular framework for controllable protein segment engineering.Protein science : a publication of the Protein Society · 2026Article
- Mechanistic Determinants of Oriented Enzyme Immobilization from Martini Simulations.The journal of physical chemistry letters · 2026Article
- Loop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Enzyme immobilization is indispensable for enhancing enzyme performance in various industrial applications. Typically, enzymes require specific spatial arrangements for optimal functionality, underscoring the importance of correct orientation. Despite well-known N- or C-terminus tailoring techniques, alternatives for achieving orientation control are limited. Here, we propose a novel approach that tailors the enzyme surface with engineered His-rich loops. To that aim, we first solve the X-ray crystal structure of a hexameric alcohol dehydrogenase from Thermus thermophilus HB27 (TtHBDH) (PDB: 9FBD). Guided by this 3D structure, we engineer the enzyme surface with a new loop enriched with six His residues to control enzyme orientation. Molecular dynamics simulations reveal that the engineered loop's imidazole rings have greater solvent accessibility than those in native His residues, allowing for more efficient enzyme immobilization on certain metal chelate-functionalized carriers. Using carriers functionalized with iron (III)-catechol, the apparent V
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Registered trials
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