학술논문
Biomimetic Mineralization of Large Enzymes Utilizing a Stable Zirconium-Based Metal-Organic Frameworks.
Document Type
Academic Journal
Author
Akpinar I; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Wang X; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Fahy K; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Sha F; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Yang S; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Kwon TW; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Das PJ; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Islamoglu T; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Farha OK; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; Department of Chemical Engineering, Northwestern University, Evanston, Illinois 60208-3113, United States.; Stoddart JF; Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113, United States.; School of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.; Stoddart Institute of Molecular Science, Department of Chemistry, Zhejiang University, Hangzhou 310027, China.; ZJU-Hangzhou Global Scientific and Technological Innovation Center Hangzhou 311215, China.
Source
Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE
Subject
Language
English
Abstract
Enzymes are natural catalysts for a wide range of metabolic chemical transformations, including selective hydrolysis, oxidation, and phosphorylation. Herein, we demonstrate a strategy for the encapsulation of enzymes within a highly stable zirconium-based metal-organic framework. UiO-66-F 4 was synthesized under mild conditions using an enzyme-compatible amino acid modulator, serine, at a modest temperature in an aqueous solution. Enzyme@UiO-66-F 4 biocomposites were then formed by an in situ encapsulation route in which UiO-66-F 4 grows around the enzymes and, consequently, provides protection for the enzymes. A range of enzymes, namely, lysozyme, horseradish peroxidase, and amano lipase, were successfully encapsulated within UiO-66-F 4 . We further demonstrate that the resulting biocomposites are stable under conditions that could denature many enzymes. Horseradish peroxidase encapsulated within UiO-66-F 4 maintained its biological activity even after being treated with the proteolytic enzyme pepsin and heated at 60 °C. This strategy expands the toolbox of potential metal-organic frameworks with different topologies or functionalities that can be used as enzyme encapsulation hosts. We also demonstrate that this versatile process of in situ encapsulation of enzymes under mild conditions (i.e., submerged in water and at a modest temperature) can be generalized to encapsulate enzymes of various sizes within UiO-66-F 4 while protecting them from harsh conditions (i.e., high temperatures, contact with denaturants or organic solvents).