Locking the Ultrasound-Induced Active Conformation of Metalloenzymes in Metal–Organic Frameworks

• DOI: 10.1021/jacs.2c06471
• Publication Date: 2022-09-09T03:10:35Z
• Authors: Jieying Liang; Muhammad Yazid Bi...; Joel Yong; Zeping Du; Zhimin Ao; Aditya Rawal; Jason A. Scott; Jeffrey R. Harmer; Joseph Wang; Kang Liang
• Keywords: 570; 34 Chemical Sciences; Bioengineering; Heme; 540; Enzymes, Immobilized; Immobilized; 01 natural sciences; anzsrc-for: 34 Chemical Sciences; Enzymes; 0104 chemical sciences; anzsrc-for: 40 Engineering; Metalloproteins; Solvents; anzsrc-for: 03 Chemical Sciences; Horseradish Peroxidase; Metal-Organic Frameworks; 40 Engineering

Enhancing the enzymatic activity inside metal-organic frameworks (MOFs) is a critical challenge in chemical technology and bio-technology, which, if addressed, will broaden their scope energy, food, environmental, pharmaceutical industries. Here, we report simple yet versatile effective strategy to optimize biocatalytic by using MOFs rapidly "lock" ultrasound (US)-activated but more fragile conformation of metalloenzymes. The results demonstrate that up 5.3-fold 9.3-fold enhancement free MOF-immobilized enzymes could be achieved compared those without US pretreatment, respectively. Using horseradish peroxidase as model, molecular dynamics simulation demonstrates improved enzyme driven an opened gate heme active site, which allows efficient substrate binding enzyme. intact site confirmed solid-state UV-vis electron paramagnetic resonance, while US-induced change circular dichroism spectroscopy Fourier-transform infrared spectroscopy. In addition, biocomposites does not compromise stability upon heating or exposure organic solvent digestion cocktail. This rapid locking immobilization gives rise new possibilities for exploitation highly biocatalysts diverse applications.