{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T02:00:54Z","timestamp":1791424854510,"version":"4.3.3"},"reference-count":76,"publisher":"Microbiology Society","issue":"10","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2003,10,1]]},"abstract":"<jats:p>\n                  <jats:italic>Rhodococcus<\/jats:italic> sp. strain MS11 was isolated from a mixed culture. It displays a diverse range of metabolic capabilities. During growth on 1,2,4-trichlorobenzene, 1,2,4,5-tetrachlorobenzene (1,2,4,5-TeCB) and 3-chlorobenzoate stoichiometric amounts of chloride were released. It also utilized all three isomeric dichlorobenzenes and 1,2,3-trichlorobenzene as the sole carbon and energy source. Furthermore, the bacterium grew well on a great number of n-alkanes ranging from n-heptane to n-triacontane and on the branched alkane 2,6,10,14-tetramethylpentadecane (pristane) and slowly on n-hexane and n-pentatriacontane. It was able to grow at temperatures from 5 to 30\u200a\u00b0C, with optimal growth at 20\u200a\u00b0C, and could tolerate 6\u200a% NaCl in mineral salts medium. Genes encoding the initial chlorobenzene dioxygenase were detected by using a primer pair that was designed against the <jats:italic>\u03b1<\/jats:italic>-subunit (TecA1) of the chlorobenzene dioxygenase of <jats:italic>Ralstonia<\/jats:italic> (formerly <jats:italic>Burkholderia<\/jats:italic>) sp. strain PS12. The amino acid sequence of the amplified part of the <jats:italic>\u03b1<\/jats:italic>-subunit of the chlorobenzene dioxygenase of <jats:italic>Rhodococcus<\/jats:italic> sp. strain MS11 showed &gt;99\u200a% identity to the <jats:italic>\u03b1<\/jats:italic>-subunit of the chlorobenzene dioxygenase from <jats:italic>Ralstonia<\/jats:italic> sp. strain PS12 and the parts of both <jats:italic>\u03b1<\/jats:italic>-subunits responsible for substrate specificity were identical. The subsequent enzymes dihydrodiol dehydrogenase and chlorocatechol 1,2-dioxygenase were induced in cells grown on 1,2,4,5-TeCB. During cultivation on medium-chain-length n-alkanes ranging from n-decane to n-heptadecane, including 1-hexadecene, and on the branched alkane pristane, strain MS11 produced biosurfactants lowering the surface tension of the cultures from 72 to \u2a7d29\u2005mN\u2005m<jats:sup>\u22121<\/jats:sup>. Glycolipids were extracted from the supernatant of a culture grown on n-hexadecane and characterized by <jats:sup>1<\/jats:sup>H- and <jats:sup>13<\/jats:sup>C-NMR-spectroscopy and mass spectrometry. The two major components consisted of <jats:italic>\u03b1<\/jats:italic>,<jats:italic>\u03b1<\/jats:italic>-trehalose esterified at C-2 or C-4 with a succinic acid and at C-2\u2032 with a decanoic acid. They differed from one another in that one 2,3,4,2\u2032-trehalosetetraester, found in higher concentration, was esterified at C-2, C-3 or C-4 with one octanoic and one decanoic acid and the other one, of lower concentration, with two octanoic acids. The results demonstrate that <jats:italic>Rhodococcus<\/jats:italic> sp. strain MS11 may be well suited for bioremediation of soils and sediments contaminated for a long time with di-, tri- and tetrachlorobenzenes as well as alkanes.<\/jats:p>","DOI":"10.1099\/mic.0.26188-0","type":"journal-article","created":{"date-parts":[[2003,10,1]],"date-time":"2003-10-01T22:57:30Z","timestamp":1065049050000},"page":"2879-2890","source":"Crossref","is-referenced-by-count":76,"title":["Degradation of alkanes and highly chlorinated benzenes, and production of biosurfactants, by a psychrophilic Rhodococcus sp. and genetic characterization of its chlorobenzene dioxygenase"],"prefix":"10.1099","volume":"149","author":[{"given":"Peter","family":"Rapp","sequence":"first","affiliation":[{"name":"GBF-National Research Centre for Biotechnology, Division of Microbiology, Mascheroderweg 1, D-38124 Braunschweig, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lotte H. 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