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      Enzyme encapsulation in metal–organic frameworks for applications in catalysis

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          Abstract

          Various methods for encapsulating enzymes in metal–organic frameworks are discussed and the catalytic activity of biocomposites prepared using these methods is highlighted.

          Abstract

          Enzymes are natural catalysts which are highly selective and efficient. Given that enzymes have very intricate and delicate structures, they need to be stabilized and protected by a support material if they are to be used under challenging catalytic conditions. This highlight focuses on the use of metal–organic frameworks as supports for enzyme encapsulation and subsequent catalytic applications. De novo and post-synthetic methods of encapsulation are discussed and the relative catalytic activities of the enzyme@MOF composites versus free enzymes are highlighted.

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          Chemical, thermal and mechanical stabilities of metal–organic frameworks

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            Biomimetic mineralization of metal-organic frameworks as protective coatings for biomacromolecules

            Enhancing the robustness of functional biomacromolecules is a critical challenge in biotechnology, which if addressed would enhance their use in pharmaceuticals, chemical processing and biostorage. Here we report a novel method, inspired by natural biomineralization processes, which provides unprecedented protection of biomacromolecules by encapsulating them within a class of porous materials termed metal-organic frameworks. We show that proteins, enzymes and DNA rapidly induce the formation of protective metal-organic framework coatings under physiological conditions by concentrating the framework building blocks and facilitating crystallization around the biomacromolecules. The resulting biocomposite is stable under conditions that would normally decompose many biological macromolecules. For example, urease and horseradish peroxidase protected within a metal-organic framework shell are found to retain bioactivity after being treated at 80 °C and boiled in dimethylformamide (153 °C), respectively. This rapid, low-cost biomimetic mineralization process gives rise to new possibilities for the exploitation of biomacromolecules.
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              Industrial use of immobilized enzymes.

              Although many methods for enzyme immobilization have been described in patents and publications, relatively few processes employing immobilized enzymes have been successfully commercialized. The cost of most industrial enzymes is often only a minor component in overall process economics, and in these instances, the additional costs associated with enzyme immobilization are often not justified. More commonly the benefit realized from enzyme immobilization relates to the process advantages that an immobilized catalyst offers, for example, enabling continuous production, improved stability and the absence of the biocatalyst in the product stream. The development and attributes of several established and emerging industrial applications for immobilized enzymes, including high-fructose corn syrup production, pectin hydrolysis, debittering of fruit juices, interesterification of food fats and oils, biodiesel production, and carbon dioxide capture are reviewed herein, highlighting factors that define the advantages of enzyme immobilization.
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                Author and article information

                Journal
                CRECF4
                CrystEngComm
                CrystEngComm
                Royal Society of Chemistry (RSC)
                1466-8033
                2017
                2017
                : 19
                : 29
                : 4082-4091
                Affiliations
                [1 ]Department of Chemistry
                [2 ]Northwestern University
                [3 ]Evanston
                [4 ]USA
                [5 ]Argonne-Northwestern Solar Energy Research (ANSER) Center
                Article
                10.1039/C7CE00022G
                93bf46d6-19ba-47a4-beb1-3c7beb774949
                © 2017
                History

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