Intracellular Self-Immobilization of Carbonic Anhydrase Enables Carrier-Free Recovery and Stable Operation under Direct Air Capture Conditions
炭酸脱水酵素の細胞内自己固定化により、キャリアフリー回収と直接空気回収条件下での安定運用が可能に (AI 翻訳)
Zhou Deng, Zicheng Wu, Yaxin Chen, Yanhong Zhou, Manqi Cheng, Xiang Li, Feng Yu, Shiyu Lu, Zhiwei Yi, Guangya Zhang
🤖 gxceed AI 要約
日本語
本研究では、炭酸脱水酵素(CA)を直接空気回収(DAC)条件下で安定化するため、カプセリンを介した自己固定化戦略を提案。SazCAとEncMhの融合により、宿主細胞内で自己集合し、遠心分離で簡便回収可能な超分子粒子を形成。高い熱安定性と耐アルカリ性を示し、pH調整で可逆的にサイズ変換可能。DAC条件下では長期間のChlorella培養を促進し、アミノ酸塩や3級アミンなど代表的なDAC吸収剤中での安定性も向上。
English
This study proposes an encapsulin-mediated self-immobilization strategy for carbonic anhydrase (CA) stabilization under direct air capture (DAC) conditions. Fusion of SazCA with EncMh enables intracellular self-assembly into supramolecular particles, recoverable by simple centrifugation. The assemblies exhibit high thermal and alkaline stability, reversible size switching via pH, and enhance long-term Chlorella cultivation under DAC. They show improved stability in DAC absorbents (amino acid salts, tertiary amines).
Unofficial AI-generated summary based on the public title and abstract. Not an official translation.
📝 gxceed 編集解説 — Why this matters
日本のGX文脈において
日本では、CCUS技術の実用化が国のGX戦略の柱の一つであり、DACは特に注目されている。本成果は、酵素のDACプロセスへの組み込み可能性を示し、国内の材料・バイオ技術開発に参考となる。
In the global GX context
Globally, DAC is a key negative emissions technology. This study advances enzyme-based DAC systems, offering a scalable and robust approach relevant to the growing carbon removal market and regulatory frameworks (e.g., US 45Q, EU Carbon Removal Certification).
👥 読者別の含意
🔬研究者:A novel strategy for stabilizing carbonic anhydrase in DAC conditions using encapsulin self-immobilization, with implications for biocatalytic carbon capture design.
🏢実務担当者:Potential to integrate this enzyme stabilization method into scalable DAC systems, though further engineering for specific contactors is needed.
📄 Abstract（原文）
Efficient deployment of carbonic anhydrase (CA) in direct air capture (DAC) is constrained by the lack of enzyme durability under alkaline, chemically complex, and long-term operating conditions. A carrier-free self-immobilization strategy based on encapsulin-mediated intracellular assembly was proposed to address these challenges. The fusion of Sulphurihydrogenibium azorense carbonic anhydrase (SazCA) with the encapsulin EncMh from Mycolicibacterium hassiacum enables spontaneous self-assembly into supramolecular particles during expression in host cells, allowing high-yield production and low-energy recovery by simple centrifugation. The resulting SazCA-EncMh assemblies exhibit high thermal stability and broad tolerance toward alkaline and ion-rich environments. Notably, their supramolecular state can be reversibly switched between nano- and microscale assemblies by pH modulation without loss of catalytic activity over multiple cycles. Under DAC, free SazCA-EncMh significantly enhances long-term Chlorella cultivation over 21 days, indicating sustained extracellular catalytic function and improved inorganic carbon availability. In addition, SazCA-EncMh exbibits improved stability relative to ferritin-based assemblies in representative DAC absorbents, including amino acid salts and tertiary amines. Overall, encapsulin-enabled self-immobilization offers a practical and scalable strategy for stabilizing CA under DAC-relevant conditions, supporting its integration into biological and hybrid carbon capture systems.
🔗 Provenance — このレコードを発見したソース
- openalex https://doi.org/10.1021/acssuschemeng.6c01045first seen 2026-07-04 04:55:26
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