Carbonic Anhydrase-Mimicking Supramolecular Nanoassemblies for Developing Carbon Capture Membranes.

As a ubiquitous family of enzymes with high performance in converting carbon dioxide (CO) into bicarbonate, carbonic anhydrases (CAs) sparked enormous attention for carbon capture. Nevertheless, the high cost and operational instability of CAs hamper their practical relevance, and the utility of CAs is mainly limited to aqueous applications where CO-to-bicarbonate conversion is possible. Taking advantage of the chemical motif that endows CA-like active sites (metal-coordinated histidine), here we introduce a new line of high-performance gas separation membranes with CO-philic behavior.

Comparison of the stability of CYP105A1 and its variants engineered for production of active forms of vitamin D.

CYP105A1 from Streptomyces griseolus converts vitamin D3 to its biologically active form, 1α,25-dihydroxy vitamin D3. R73A/R84A mutation enhanced the 1α- and 25-hydroxylation activity for vitamin D3, while M239A mutation generated the 1α-hydroxylation activity for vitamin D2. In this study, the stability of six CYP105A1 enzymes, including 5 variants (R73A/R84A, M239A, R73A/R84A/M239A (=TriA), TriA/E90A, and TriA/E90D), was examined.