These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Enzyme Immobilization using Covalent Organic Frameworks: From Synthetic Strategy to COFs Functional Role. Author: Fan X, Zhai S, Xue S, Zhi L. Journal: ACS Appl Mater Interfaces; 2024 Aug 07; 16(31):40371-40390. PubMed ID: 39072501. Abstract: Enzymes, a class of biocatalysts, exhibit remarkable catalytic efficiency, specificity, and selectivity, governing many reactions that are essential for various cascades within living cells. The immobilization of structurally flexible enzymes on appropriate supports holds significant importance in facilitating biomimetic transformations in extracellular environments. Covalent organic frameworks (COFs) have emerged as ideal candidates for enzyme immobilization due to high surface tunability, diverse chemical/structural designs, exceptional stability, and metal-free nature. Various immobilization techniques have been proposed to fabricate COF-enzyme biocomposites, offering significant enhancements in activity and reusability for COF-immobilized enzymes as well as new insights into developing advanced enzyme-based applications. In this review, we provide a comprehensive overview of state-of-the-art strategies for immobilizing enzymes within COFs by focusing on their applicability and versatility. These strategies are systematically summarized and compared by categorizing them into postsynthesis immobilization and in situ immobilization, where their respective strengths and limitations are thoroughly discussed. Combined with an overview of critical emerging applications, we further elucidate the multifaceted roles of COFs in enzyme immobilization and subsequent applications, highlighting the advanced biofunctionality achievable through COFs.[Abstract] [Full Text] [Related] [New Search]