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CAs form a family of metalloenzymes that catalyze hydration of CO<jats:sub>2<\/jats:sub>\/interconversion between CO<jats:sub>2<\/jats:sub> and water to bicarbonate ions and protons. They are divided into eight independent gene families (\u03b1, \u03b2, \u03b3, \u03b4, \u03b6, \u03b7, \u03b8, and \u03b9). Interestingly, many pathogens have been identified with only \u03b2- and\/or \u03b3-CAs, which can be targeted with CA-specific inhibitors (CAIs) acting as anti-pathogen drugs. Since it is important to study the potential off-target effects of CAIs for both the human body and its commensal bacteria, we took <jats:italic>L. rhamnosus<\/jats:italic> GG as our study subject. To date, only a single \u03b1-CA has been identified in <jats:italic>L. rhamnosus<\/jats:italic> GG, which was successfully produced and biochemically characterized. LrhCA showed moderate catalytic activity with the following kinetic parameters: k<jats:sub>cat<\/jats:sub> of 9.86\u2009\u00d7\u200910<jats:sup>5<\/jats:sup>\u00a0s<jats:sup>\u22121<\/jats:sup> and k<jats:sub>cat<\/jats:sub>\/K<jats:sub>M<\/jats:sub> of 1.41\u2009\u00d7\u200910<jats:sup>7<\/jats:sup>\u00a0s<jats:sup>\u22121<\/jats:sup>\u00a0M<jats:sup>\u22121<\/jats:sup>. Moderate inhibition was established with 11 of the 39 studied sulfonamides. The best inhibitors were 5-((4-aminophenyl)sulfonamido)-1,3,4-thiadiazole-2-sulfonamide, 4-(2-hydroxymethyl-4-nitrophenyl-sulfonamidoethyl)-benzenesulfonamide, and benzolamide with <jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub> values of 319\u00a0nM, 378\u00a0nM, and 387\u00a0nM, respectively. The other compounds showed weaker inhibitory effects. The <jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub> of acetazolamide, a classical CAI, was 733\u00a0nM. In vitro experiments with acetazolamide showed that it had no significant effect on cell growth in <jats:italic>L. rhamnosus<\/jats:italic> GG culture. Several sulfonamides, including acetazolamide, are in use as clinical drugs, making their inhibition data highly relevant to avoid any adverse off-target effects towards the human body and its probiotic organisms.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Key points<\/jats:title>\n                <jats:p>\u2022 <jats:italic>The \u03b1-carbonic anhydrase from Lactobacillus rhamnosus GG (LrhCA) is 24.3\u00a0kDa.<\/jats:italic><\/jats:p>\n                <jats:p>\u2022 <jats:italic>LrhCA has significant catalytic activity with a kcat of 9.9\u2009\u00d7\u2009105\u00a0s-1<\/jats:italic>.<\/jats:p>\n                <jats:p>\u2022 <jats:italic>Acetazolamide resulted in a marginal inhibitory effect on cell growth<\/jats:italic>.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1007\/s00253-022-11990-3","type":"journal-article","created":{"date-parts":[[2022,5,25]],"date-time":"2022-05-25T10:03:13Z","timestamp":1653472993000},"page":"4065-4074","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["The production and biochemical characterization of \u03b1-carbonic anhydrase from Lactobacillus rhamnosus GG"],"prefix":"10.1007","volume":"106","author":[{"given":"Linda J.","family":"Urba\u0144ski","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia","family":"Bua","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Angeli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reza Zolfaghari","family":"Emameh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harlan R.","family":"Barker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marianne","family":"Kuuslahti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vesa P.","family":"Hyt\u00f6nen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seppo","family":"Parkkila","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,5,25]]},"reference":[{"issue":"7","key":"11990_CR1","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1002\/bip.22456","volume":"101","author":"V Alterio","year":"2014","unstructured":"Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G (2014) The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors. 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