Protein Immobilization in Metal–Organic Frameworks by Covalent Binding
Xuan Wang A , Tegan A. Makal B and Hong-Cai Zhou A CA Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
B Department of Natural Sciences, The University of Virginia’s College at Wise, Wise, VA 24293, USA.
C Corresponding author. Email: zhou@chem.tamu.edu
Australian Journal of Chemistry 67(11) 1629-1631 https://doi.org/10.1071/CH14104
Submitted: 5 March 2014 Accepted: 4 June 2014 Published: 21 August 2014
Abstract
Metal–organic frameworks (MOFs), possessing a well defined system of pores, demonstrate extensive potential serving as a platform in biological catalysis. Successful immobilization of enzymes in a MOF system retains the enzymatic activity, renders the active site more accessible to the substrate, and promises recyclability for reuse, and solvent adaptability in a broad range of working conditions. This highlight describes enzyme immobilization on MOFs via covalent binding and its significance.
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