{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T14:57:09Z","timestamp":1790261829222,"version":"4.1.0"},"reference-count":27,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2005,7,1]],"date-time":"2005-07-01T00:00:00Z","timestamp":1120176000000},"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":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2005,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            To find microorganisms that could reduce phenyl trifluoromethyl ketone (PTK) to (\n            <jats:italic>S<\/jats:italic>\n            )-1-phenyltrifluoroethanol [(\n            <jats:italic>S<\/jats:italic>\n            )-PTE], styrene-assimilating bacteria (ca. 900 strains) isolated from soil samples were screened. We found that\n            <jats:italic>Leifsonia<\/jats:italic>\n            sp. strain S749 was the most suitable strain for the conversion of PTK to (\n            <jats:italic>S<\/jats:italic>\n            )-PTE in the presence of 2-propanol as a hydrogen donor. The enzyme corresponding to the reaction was purified homogeneity, characterized and designated\n            <jats:italic>Leifsonia<\/jats:italic>\n            alcohol dehydrogenase (LSADH). The purified enzyme had a molecular weight of 110,000 and was composed of four identical subunits (molecular weight, 26,000). LSADH required NADH as a cofactor, showed little activity with NADPH, and reduced a wide variety of aldehydes and ketones. LSADH catalyzed the enantioselective reduction of some ketones with high enantiomeric excesses (e.e.): PTK to (\n            <jats:italic>S<\/jats:italic>\n            )-PTE (&gt;99% e.e.), acetophenone to (\n            <jats:italic>R<\/jats:italic>\n            )-1-phenylethanol (99% e.e.), and 2-heptanone to (\n            <jats:italic>R<\/jats:italic>\n            )-2-heptanol (&gt;99% e.e.) in the presence of 2-propanol without an additional NADH regeneration system. Therefore, it would be a useful biocatalyst.\n          <\/jats:p>","DOI":"10.1128\/aem.71.7.3633-3641.2005","type":"journal-article","created":{"date-parts":[[2005,7,7]],"date-time":"2005-07-07T06:37:11Z","timestamp":1120718231000},"page":"3633-3641","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":76,"title":["Purification and Characterization of a Novel Alcohol Dehydrogenase from\n            <i>Leifsonia<\/i>\n            sp. Strain S749: a Promising Biocatalyst for an Asymmetric Hydrogen Transfer Bioreduction"],"prefix":"10.1128","volume":"71","author":[{"given":"Kousuke","family":"Inoue","sequence":"first","affiliation":[{"name":"Biotechnology Research Center, Toyama Prefectural University, Kosugi, Toyama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshihide","family":"Makino","sequence":"additional","affiliation":[{"name":"Biotechnology Research Center, Toyama Prefectural University, Kosugi, Toyama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nobuya","family":"Itoh","sequence":"additional","affiliation":[{"name":"Biotechnology Research Center, Toyama Prefectural University, Kosugi, Toyama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0079-6107(97)00020-5"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1021\/jo00031a036","volume":"57","year":"1992","unstructured":"Bradshaw, C. 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