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Molecules 2014, 19(7), 10103-10114; doi:10.3390/molecules190710103
Article

Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes

1
, 1,2,*  and 2
Received: 6 May 2014; in revised form: 19 June 2014 / Accepted: 3 July 2014 / Published: 10 July 2014
(This article belongs to the Section Metabolites)
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Abstract: Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO2) and water (H2O) into a proton (H+) and bicarbonate (HCO3) ion. On the other hand, capsaicin is the main component in hot chili peppers and is used extensively used in spices, food additives and drugs; it is responsible for their spicy flavor and pungent taste. There are sixteen known CA isoforms in humans. Human CA isoenzymes I, and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of capsaicin against the slow cytosolic isoform hCA I, and the ubiquitous and dominant rapid cytosolic isozymes hCA II were studied. Both CA isozymes were inhibited by capsaicin in the micromolar range. This naturally bioactive compound has a Ki of 696.15 µM against hCA I, and of 208.37 µM against hCA II.
Keywords: capsaicin; carbonic anhydrase; enzyme purification; enzyme inhibition; affinity chromatography capsaicin; carbonic anhydrase; enzyme purification; enzyme inhibition; affinity chromatography
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Arabaci, B.; Gulcin, I.; Alwasel, S. Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes. Molecules 2014, 19, 10103-10114.

AMA Style

Arabaci B, Gulcin I, Alwasel S. Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes. Molecules. 2014; 19(7):10103-10114.

Chicago/Turabian Style

Arabaci, Betul; Gulcin, Ilhami; Alwasel, Saleh. 2014. "Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes." Molecules 19, no. 7: 10103-10114.



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