{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T10:09:23Z","timestamp":1790935763267,"version":"4.1.0"},"reference-count":55,"publisher":"S. Karger AG","issue":"4","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microb Physiol"],"published-print":{"date-parts":[[2009]]},"abstract":"<jats:p>A tyrosinase-expressing bacterium was isolated from soil, and extracellular enzymatic activity was induced by the presence of tyrosine and CuSO&lt;sub&gt;4&lt;\/sub&gt;. Amplification of the 16S rDNA genes revealed a high similarity with &lt;i&gt;Bacillus megaterium&lt;\/i&gt;. The enzyme was over-expressed in &lt;i&gt;Escherichia coli &lt;\/i&gt;BL21 and purified using an affinity column. The tyrosinase was composed of 297 amino acids and was determined to be a monomer with a relative molecular mass of 31 kDa according to gel filtration. The &lt;i&gt;K&lt;\/i&gt;&lt;sub&gt;m&lt;\/sub&gt; values for 3,4-dihydroxy-&lt;i&gt;L&lt;\/i&gt;-phenylalanine (&lt;i&gt;L&lt;\/i&gt;-DOPA) and &lt;i&gt;L&lt;\/i&gt;-tyrosine were 0.35 and 0.075 m&lt;i&gt;M&lt;\/i&gt;, respectively, and the &lt;i&gt;k&lt;\/i&gt;&lt;sub&gt;cat&lt;\/sub&gt;\/&lt;i&gt;K&lt;\/i&gt;&lt;sub&gt;m&lt;\/sub&gt; values were 28.9\u00b710&lt;sup&gt;3&lt;\/sup&gt; and 32.9\u00b710&lt;sup&gt;3&lt;\/sup&gt; (s&lt;sup&gt;\u20131&lt;\/sup&gt;\u00b7&lt;i&gt;M&lt;\/i&gt;&lt;sup&gt;\u20131&lt;\/sup&gt;). The maximum activity for both monophenolase and diphenolase was observed at 50\u00b0C and pH 7.0. Enzymatic activity was enhanced in the presence of 10\u201350% water-miscible organic solvents, which included ethanol, methanol, 2-propanol and dimethyl sulfoxide (DMSO). The activity in 30% DMSO was 170% of the activity in water and the enantioselectivity towards &lt;i&gt;L&lt;\/i&gt;-DOPA decreased by 40%. The residual activity following an incubation period of 17 h in 0\u201370% methanol was constant. This newly isolated and characterized tyrosinase may have potential applications in organic synthesis due to its high activity and stability at typically denaturing conditions.<\/jats:p>","DOI":"10.1159\/000233506","type":"journal-article","created":{"date-parts":[[2009,8,7]],"date-time":"2009-08-07T13:46:22Z","timestamp":1249652782000},"page":"188-200","source":"Crossref","is-referenced-by-count":73,"title":["Isolation, Cloning and Characterization of a Tyrosinase with Improved Activity in Organic Solvents from &lt;i&gt;Bacillus 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