
Enzyme Captures Carbon
Thermostabilized enzyme created for biofuels production
Zoë Fisher of Bioenergy and Environmental Science (B-8) and collaborators from the University of Florida have created an enzyme that has the ability to capture carbon with much greater efficiency. The paper, which describes thermally stabilized human carbonic anhydrase II (HCA II), was published in the journal Protein Engineering: Design and Selection and featured on the cover. Carbonic anhydrases (CAs) are ubiquitous enzymes that regulate the interconversion of carbon dioxide (CO2) and bicarbonate. Within the human body, carbonic anhydrases control the acid-base balance in the blood and enable transport of CO2 out of tissue. HCA II is one of the fastest enzymes ever studied. These enzymes might serve as biocatalysts for carbon sequestration and biofuel production if they could function under harsh industrial conditions. Therefore, the researchers developed HCA II variants with enhanced thermostability while retaining high solubility and catalytic activity.
Zoë Fisher
Dr. Fisher's research interests are varied and range from algae-derived biofuels to structural enzymology of carbonic anhydrase. She takes a multi-disciplinary approach to the study of complicated enzyme mechanisms, combining NMR spectroscopy with X-ray and neutron diffraction to understand the role of specific active site amino acids. Dr. Fisher has published 40 papers in the fields of biochemistry, structural biology, X-ray and neutron crystallography, mass spectrometry, enzyme kinetics, and molecular biology.
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