Three 1‐aminoindanes, four anilines and BnOH or t‐BuOH were reacted with chlorosulfonyl isocyanate to give sulfamoyl carbamates. Pd‐C catalysed hydrogenolysis reactions of carbamates or deprotection of the Boc group of the carbamates with CF3CO2H afforded seven novel sulfamides. Human carbonic anhydrase (hCA) isoenzymes I and II (hCA I and hCA II) were purified from fresh human blood erythrocytes with one‐step affinity chromatography on Sepharose 4B‐tyrosine‐sulfanilamide. The inhibitory properties of the novel sulfamides on both isoenzymes were determined using the esterase activity with 4‐nitrophenyl acetate (NPA) as substrate. The tested novel sulfamides derived from 1‐aminoindanes and anilines effectively inhibited hCA I and II competitively in the nanomolar range. Among these compounds, the novel sulfamide derivative 17 showed the most potent inhibitory effect against hCA I (Ki: 153.88 nM), while sulfamide derivative 26 showed the highest inhibitory potential against hCA II (Ki: 117.80 nM).