Stability-Controllable Self-Immobilization of Carbonic Anhydrase Fused with a Silica-Binding Tag onto Diatom Biosilica for Enzymatic CO2 Capture and Utilization
- 주제(키워드) carbonic anhydrase , silica-binding tag , biosilica , Hydrogenovibrio marinus , enzyme immobilization , mactomolecular crowding
- 주제(기타) Nanoscience & Nanotechnology
- 주제(기타) Materials Science, Multidisciplinary
- 설명문(일반) [Jo, Byung Hoon] Gyeongsang Natl Univ, Div Life Sci, Jinju 52828, South Korea; [Jo, Byung Hoon] Gyeongsang Natl Univ, Res Inst Life Sci, Jinju 52828, South Korea; [Kim, Suhyeok; Joo, Kye Il; Cha, Hyung Joon] Pohang Univ Sci & Technol, Dept Chem Engn, Pohang 37673, South Korea
- 관리정보기술 faculty
- 등재 SCIE, SCOPUS
- 발행기관 AMER CHEMICAL SOC
- 발행년도 2020
- URI http://www.dcollection.net/handler/ewha/000000182486
- 본문언어 영어
- Published As http://dx.doi.org/10.1021/acsami.0c03804
초록/요약
Exploiting carbonic anhydrase (CA), an enzyme that catalyzes the hydration of CO2, is a powerful route for ecofriendly and cost-effective carbon capture and utilization. For successful industrial applications, the stability and reusability of CA should be improved, which necessitates enzyme immobilization. Herein, the ribosomal protein L2 (Si-tag) from Escherichia coli was utilized for the immobilization of CA onto diatom biosilica, a promising renewable support material. The Si-tag was redesigned (L2NC) and genetically fused to CA from the marine bacterium Hydrogenovibrio marinus (hmCA). One-step self-immobilization of hmCA-L2NC onto diatom biosilica by simple mixing was successfully achieved via Si-tag-mediated strong binding, showing multilayer adsorption with a maximal loading of 1.4 wt %. The immobilized enzyme showed high reusability and no enzyme leakage even under high temperature conditions. The activity of hmCA-L2NC was inversely proportional to the enzyme loading, while the stability was directly proportional to the enzyme loading. This discovered activity-stability trade-off phenomenon could be attributed to macromolecular crowding on the highly dense surface of the enzyme-immobilized biosilica. Collectively, our system not only facilitates the stability-controllable self-immobilization of enzyme via Si-tag on a diatom biosilica support for the robust, facile, and green construction of stable biocatalysts, but is also a unique model for studying the macromolecular crowding effect on surface-immobilized enzymes.
more