High expression and biosilica encapsulation of alkaline-active carbonic anhydrase for CO2 sequestration system development

Design of a Superpositively Charged Enzyme: Human Carbonic Anhydrase II Variant with Ferritin Encapsulation and Immobilization

“…With thermally stable CAs from other organisms, encapsulation at room temperature results in only 60% retention of activity. 51,90,91 The highest activity upon encapsulation was a recent report showing 85% activity with a GFP(+36)−hCAII fusion. 36 Here, we explore the exciting potential to encapsulate hCAII in a stable ferritin protein scaffold, by engineering complementary surface charge interactions to favor encapsulation and robust enzyme activity.…”

“…We have also shown simpler methods of loading as AfFtn can self-assemble around gold nanoparticles with complementary diameter and surface ligands, without requiring additional reagents. − One major advantage of encapsulation within AfFtn is that it can confer additional thermal stability to the cargo. , A general, one-step method for incorporating an enzyme within AfFtn would greatly expand the utility of this approach for enzyme immobilization. With thermally stable CAs from other organisms, encapsulation at room temperature results in only 60% retention of activity. ,, The highest activity upon encapsulation was a recent report showing 85% activity with a GFP­(+36)–hCAII fusion . Here, we explore the exciting potential to encapsulate hCAII in a stable ferritin protein scaffold, by engineering complementary surface charge interactions to favor encapsulation and robust enzyme activity.…”

“…In addition, using hCAII in industrial applications requires enzyme immobilization as free enzyme cannot be recycled from the reaction . The efficiency of enzymes, including hCAII, is decreased upon immobilization via current methods involving adsorption, covalent cross-linking, entrapment, , and encapsulation within a supramolecular host . Using other robust proteins to protect or sequester enzymes provides a route to retaining enzyme activity in harsh environments while facilitating immobilization or recovery of the associated enzymes.…”

Modular Catalysis: Aptamer Enhancement of Enzyme Kinetics in a Nanoparticle Reactor

“…We sought to explore whether the substrate binding and chemistry functions of an enzymatic reaction could be partially separated by colocalization of a substrate-binding DNA aptamer and a substrate-converting enzyme inside the confines of a stable virus-like particle (VLP) shell. Encapsulation of enzymes in a wide variety of nanocompartments, including liposomes, polymersomes, nucleic acid cages, carbohydrates, hydrogels, mineral capsules, and VLPs, has been described, mostly to aid in enzyme stabilization. , In many of these cases, no or only modest decreases in enzyme activity (often defined as k cat / K M ) are observed while stability is enhanced. ,− However, few examples of rate improvement upon encapsulation have been reported, including the use of DNA nanostructures , and alginate- or carboxy­methylcellulose-coated silica …”

Carbon Dioxide Sequestration by Microbial Carbonic Anhydrases From Submarine Hydrothermal Systems

“…Continuous increases in carbon dioxide (CO 2 ) concentrations have significantly affected the environment and climate, with the current global atmospheric CO 2 levels reaching nearly 420 ppm (Min et al, 2016;Schweitzer et al, 2021). The estimated value for global CO 2 emissions is about 48 gigatons per year, and the CO 2 emissions must be reduced to < 5 gigatons per year by 2050 to achieve the goal of limiting global temperature rise to 2°C by 2100 (Valluri et al, 2022).…”