Abstract
Carbonic anhydrase (CA) is an enzyme of high interest due to its high implications relative to the medical and environmental sectors. In the current paper, an enzyme assay for the determination of CA activity is proposed and it is characterized by its simplicity and high practicability. It permits the straightforward comparison of CAs performance in physiological conditions. The methodology and the theoretical background of the evaluation method are explained in detail. Moreover, the presumed advantages over alternative assays are discussed. The assay has proven to be particularly useful for the screening of CA activity with respect to their application in CO2, capturing processes for further utilization or storage.
Highlights
Carbonic anhydrases (CAs; EC 4.2.1.1) are a group of metalloenzymes that catalyze the inter-conversion of carbon dioxide and water into the bicarbonate ion and a proton.First isolated in 1933, CAs have been found to be abundant in algae, bacteria, archaea, plants and animal tissues [1,2]
Conclusions development of CO2 capturing technologies is of high interest
2 levels in the atmosphere, application, enhancement is relative one of the options improve efficiency of this the development of capturing technologies is of high interest
Summary
Carbonic anhydrases (CAs; EC 4.2.1.1) are a group of metalloenzymes that catalyze the inter-conversion of carbon dioxide and water into the bicarbonate ion and a proton. Six different and evolutionarily unrelated classes have been identified, namely α, β, γ, δ, ζ and η [3] Despite their structural differences, all CAs utilize the same catalytic mechanism involving a central metal (mostly zinc) atom [4]. The release of nitrophenol, which is a chromophore with two characteristic adsorption peaks, through the hydrolysis of p-nitrophenol acetate is followed by spectrophotometric measurement [12] This performable test is a valuable tool allowing the rapid comparison of CA activities. There is no doubt that the application of such high end methods is well justified to address specific scientific questions, e.g., the measurement of undisturbed enzyme activity and its physiological effects in animal or plant tissues. Background and method development are explained in detail and data interpretation in terms of kinetic constants are discussed
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