The development of efficient catalytic systems is a fundamental aspect for the straightforward production of chemicals. During the last years, covalent organic frameworks (COFs) emerged as an exciting class of organic nanoporous materials. Due to their pre-designable structure, they can be prepared with distinct physicochemical characteristics, specific pore sizes, and tunable functional groups. Moreover, associated with their stability in different media, these materials are considered promising supports for enzyme immobilization. Herein, it is highlighted the recent literature of enzyme immobilization in COFs, the main immobilization strategies, and the catalytic applications of these composites.
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http://dx.doi.org/10.1002/cplu.202000549 | DOI Listing |
Bioconjug Chem
January 2025
Department of Biochemistry, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.
l-Asparaginase (l-ASNase) catalyzes the hydrolysis of l-asparagine, leading to its depletion and subsequent effects on the cellular proliferation and survival. In contrast to normal cells, malignant cells that lack asparagine synthase are extremely susceptible to asparagine deficiency. l-ASNase has been successfully employed in treating pediatric leukemias and non-Hodgkin lymphomas; however, its usage in adult patients and other types of cancer is limited due to significant side effects and drug resistance.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Sun Yat-Sen University, School of Chemistry, 135 Xingang West, 510275, Guangzhou, CHINA.
Integrating enzymes with reticular frameworks offers promising avenues for access to functionally tailorable biocatalysis. This Minireview explores recent advances in enzyme-reticular frameworks hybrid biocomposites, focusing on the utilization of porous reticular frameworks, including metal-organic frameworks, covalent-organic frameworks, and hydrogen-bonded organic frameworks, to regulate the reactivity of an enzyme encapsulated inside mainly by pore infiltration and in situ encapsulation strategies. We highlight how pore engineering and host-guest interfacial interactions within reticular frameworks create tailored microenvironments that substantially impact the mass transfer and enzyme's conformation, leading to biocatalytic rate enhancement, or imparting enzyme with non-native biocatalytic functions including substrate-selectivity and new activity.
View Article and Find Full Text PDFBiophys Physicobiol
September 2024
Faculty of Pharmaceutical Sciences, Hokkaido University of Science, Sapporo, Hokkaido 006-8585, Japan.
Biolayer interferometry (BLI) is an optical sensor-based analytical method primarily used for analyzing interactions between biomolecules. In this study, we explored the application of BLI to observe the cleavage reaction of glutathione S-transferase (GST)-tagged fusion protein by human rhinovirus (HRV) 3C protease on a BLI sensor as a new application of the BLI method. The soluble domain of the Tic22 protein from was expressed and purified as a GST-tagged fusion protein, GST-Tic22, in .
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
State Key Laboratory of Analytical Chemistry for Life Science, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, 163 Xianlin Road, Nanjing 210023, China.
Covalent modification of cell membranes has shown promise for tumor imaging and therapy. However, existing membrane labeling techniques face challenges such as slow kinetics and poor selectivity for cancer cells, leading to off-target effects and suboptimal efficacy. Here, we present an enzyme-triggered self-immobilization labeling strategy, termed E-SIM, which enables rapid and selective labeling of tumor cell membranes with bioorthogonal trans-cycloctene (TCO) handles .
View Article and Find Full Text PDFJ Biotechnol
January 2025
Analysis and Testing Center, Nanjing Normal University, Nanjing, 210023, China. Electronic address:
Chondroitin sulfate (CS) is a structurally complex anionic polysaccharide widely used in medical, cosmetic and food applications. Enzymatic catalysis is an important strategy for synthesizing CS with uniform chain lengths and well-defined structures. However, the industrial application of glycosyltransferases is hindered by limitations such as low expression yields, poor stability, and challenges in reuse.
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