{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T01:58:37Z","timestamp":1781661517437,"version":"3.54.5"},"reference-count":27,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2002,6,1]],"date-time":"2002-06-01T00:00:00Z","timestamp":1022889600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2002,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The BlaB metallo-\u03b2-lactamase of\n            <jats:italic>Chryseobacterium meningosepticum<\/jats:italic>\n            CCUG4310 was overproduced in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            by means of a T7 promoter-based expression system. The overproducing system, scaled up in a 15-liter fermentor, yielded approximately 10 mg of BlaB protein per liter, mostly released in the culture supernatant. The enzyme was purified by two ion-exchange chromatographic steps with an overall yield of 66%. Analysis of the kinetic parameters revealed efficient activities (\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>cat<\/jats:sub>\n            \/\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            ratios of &gt;10\n            <jats:sup>6<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            ) toward most penam and carbapenem compounds, with the exception of the 6-\u03b1-methoxypenam derivative temocillin and of biapenem, which were poorer substrates. Hydrolysis of cephalosporins was overall less efficient, with a remarkable variability that was largely due to variable affinities of the BlaB enzyme for different compounds. BlaB was also able to hydrolyze serine-\u03b2-lactamase inhibitors, including \u03b2-iodopenicillanate, sulbactam and, although less efficiently, tazobactam.\n          <\/jats:p>","DOI":"10.1128\/aac.46.6.1921-1927.2002","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:09:29Z","timestamp":1027764569000},"page":"1921-1927","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":27,"title":["Overproduction and Biochemical Characterization of the\n            <i>Chryseobacterium meningosepticum<\/i>\n            BlaB Metallo-\u03b2-Lactamase"],"prefix":"10.1128","volume":"46","author":[{"given":"Sandrine","family":"Vessillier","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 di L'Aquila, I-67100 L'Aquila"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Denis","family":"Docquier","sequence":"additional","affiliation":[{"name":"Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Universita\u0300 di Siena, I-53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandrine","family":"Rival","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Biochemie, Gebande 6, Universita\u0308t des Saarlandes, 66123 Saarbru\u0308cken, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Frere","sequence":"additional","affiliation":[{"name":"Laboratoire d'Enzymologie and Centre d'Inge\u0301nierie des Prote\u0301ines, Institut de Chimie, Universite\u0301 de Lie\u0300ge, Sart Tilman, B-4000 Lie\u0300ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[{"name":"Laboratoire d'Enzymologie and Centre d'Inge\u0301nierie des Prote\u0301ines, Institut de Chimie, Universite\u0301 de Lie\u0300ge, Sart Tilman, B-4000 Lie\u0300ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gianfranco","family":"Amicosante","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 di L'Aquila, I-67100 L'Aquila"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gian Maria","family":"Rossolini","sequence":"additional","affiliation":[{"name":"Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Universita\u0300 di Siena, I-53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicola","family":"Franceschini","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 di L'Aquila, I-67100 L'Aquila"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.44.11.3028-3034.2000"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3310703"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1086\/514922"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4615-4897-3_5"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.6.1211"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1107\/S0907444997010627","volume":"54","year":"1998","unstructured":"Carfi, A., E. 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