Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol
A recombinant alcohol dehydrogenase (ADH) from Kangiella koreensis was purified as a 40 kDa dimer with a specific activity of 21.3 nmol min⁻¹ mg⁻¹, a Kₘof 1.8 μM, and a kcₐₜof 1.7 min⁻¹for all-trans-retinal using NADH as cofactor. The enzyme showed activity for all-trans-retinol using NAD ⁺ as a cof...
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| Veröffentlicht in: | Biotechnology letters 2015-04, Vol.37 (4), p.849-856 |
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| creator | Hong, Seung-Hye Ngo, Ho-Phuong-Thuy Kang, Lin-Woo Oh, Deok-Kun |
| description | A recombinant alcohol dehydrogenase (ADH) from Kangiella koreensis was purified as a 40 kDa dimer with a specific activity of 21.3 nmol min⁻¹ mg⁻¹, a Kₘof 1.8 μM, and a kcₐₜof 1.7 min⁻¹for all-trans-retinal using NADH as cofactor. The enzyme showed activity for all-trans-retinol using NAD ⁺ as a cofactor. The reaction conditions for all-trans-retinol production were optimal at pH 6.5 and 60 °C, 2 g enzyme l⁻¹, and 2,200 mg all-trans-retinal l⁻¹in the presence of 5 % (v/v) methanol, 1 % (w/v) hydroquinone, and 10 mM NADH. Under optimized conditions, the ADH produced 600 mg all-trans-retinol l⁻¹after 3 h, with a conversion yield of 27.3 % (w/w) and a productivity of 200 mg l⁻¹ h⁻¹. This is the first report of the characterization of a bacterial ADH for all-trans-retinal and the biotechnological production of all-trans-retinol using ADH. |
| doi_str_mv | 10.1007/s10529-014-1740-x |
| format | Article |
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The enzyme showed activity for all-trans-retinol using NAD ⁺ as a cofactor. The reaction conditions for all-trans-retinol production were optimal at pH 6.5 and 60 °C, 2 g enzyme l⁻¹, and 2,200 mg all-trans-retinal l⁻¹in the presence of 5 % (v/v) methanol, 1 % (w/v) hydroquinone, and 10 mM NADH. Under optimized conditions, the ADH produced 600 mg all-trans-retinol l⁻¹after 3 h, with a conversion yield of 27.3 % (w/w) and a productivity of 200 mg l⁻¹ h⁻¹. This is the first report of the characterization of a bacterial ADH for all-trans-retinal and the biotechnological production of all-trans-retinol using ADH.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-014-1740-x</identifier><identifier>PMID: 25481533</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Alcanivoraceae - enzymology ; Alcanivoraceae - genetics ; Alcanivoraceae - isolation & purification ; Alcohol dehydrogenase ; Alcohol Dehydrogenase - chemistry ; Alcohol Dehydrogenase - genetics ; Alcohol Dehydrogenase - metabolism ; Amino Acid Sequence ; Applied Microbiology ; Bacteria ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Coenzymes - metabolism ; Conversion ; Dehydrogenase ; Dermatology ; Enzyme Stability ; Enzymes ; Hydrogen-Ion Concentration ; hydroquinone ; Hydroquinones - metabolism ; Kinetics ; Life Sciences ; methanol ; Methanol - metabolism ; Methyl alcohol ; Microbiology ; Molecular Sequence Data ; Molecular Weight ; NAD (coenzyme) ; NAD - metabolism ; NADH ; Optimization ; Original Research Paper ; Phylogeny ; Protein Multimerization ; Recombinant ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; Skin diseases ; Temperature ; Vitamin A - metabolism</subject><ispartof>Biotechnology letters, 2015-04, Vol.37 (4), p.849-856</ispartof><rights>Springer Science+Business Media Dordrecht 2014</rights><rights>Springer Science+Business Media Dordrecht 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-115c27d75e744c5093f1630567cb85c17ffb9da61f7a2bb5e54c299ca76512793</citedby><cites>FETCH-LOGICAL-c532t-115c27d75e744c5093f1630567cb85c17ffb9da61f7a2bb5e54c299ca76512793</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-014-1740-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-014-1740-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25481533$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hong, Seung-Hye</creatorcontrib><creatorcontrib>Ngo, Ho-Phuong-Thuy</creatorcontrib><creatorcontrib>Kang, Lin-Woo</creatorcontrib><creatorcontrib>Oh, Deok-Kun</creatorcontrib><title>Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>A recombinant alcohol dehydrogenase (ADH) from Kangiella koreensis was purified as a 40 kDa dimer with a specific activity of 21.3 nmol min⁻¹ mg⁻¹, a Kₘof 1.8 μM, and a kcₐₜof 1.7 min⁻¹for all-trans-retinal using NADH as cofactor. The enzyme showed activity for all-trans-retinol using NAD ⁺ as a cofactor. The reaction conditions for all-trans-retinol production were optimal at pH 6.5 and 60 °C, 2 g enzyme l⁻¹, and 2,200 mg all-trans-retinal l⁻¹in the presence of 5 % (v/v) methanol, 1 % (w/v) hydroquinone, and 10 mM NADH. Under optimized conditions, the ADH produced 600 mg all-trans-retinol l⁻¹after 3 h, with a conversion yield of 27.3 % (w/w) and a productivity of 200 mg l⁻¹ h⁻¹. This is the first report of the characterization of a bacterial ADH for all-trans-retinal and the biotechnological production of all-trans-retinol using ADH.</description><subject>Alcanivoraceae - enzymology</subject><subject>Alcanivoraceae - genetics</subject><subject>Alcanivoraceae - isolation & purification</subject><subject>Alcohol dehydrogenase</subject><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Alcohol Dehydrogenase - genetics</subject><subject>Alcohol Dehydrogenase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Applied Microbiology</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Coenzymes - metabolism</subject><subject>Conversion</subject><subject>Dehydrogenase</subject><subject>Dermatology</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Hydrogen-Ion Concentration</subject><subject>hydroquinone</subject><subject>Hydroquinones - metabolism</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>methanol</subject><subject>Methanol - metabolism</subject><subject>Methyl alcohol</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>NAD (coenzyme)</subject><subject>NAD - metabolism</subject><subject>NADH</subject><subject>Optimization</subject><subject>Original Research Paper</subject><subject>Phylogeny</subject><subject>Protein Multimerization</subject><subject>Recombinant</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Skin diseases</subject><subject>Temperature</subject><subject>Vitamin A - metabolism</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkkuPFCEUhYnROD2jP8CNkriZDcrlUTRL0_EVJ3GhsyYUBd2M1dBCVTLtr5dOjY-4MLMgd3G_cy6XA0LPgL4CStXrClQyTSgIAkpQcvsArUAqTjqluodo1RpApNDsDJ3XekMp1Yqqx-iMSbEGyfkKHTc7W6ybfIk_7BRzwjlgO7q8yyMe_O44lLz1yVaPQ8l7_MmmbfTjaPG3XLxPNVZs04Dj1OrhMEa3uEwZH0oeZvfHcyRTsamS4qeY8vgEPQp2rP7pXb1A1-_eft18IFef33_cvLkiTnI2EQDpmBqU9EoIJ6nmATpOZadcv5YOVAi9HmwHQVnW99JL4ZjWzqpOAlOaX6DLxbfd5_vs62T2sbrTCsnnuRpoj6WBcs7ug3KuJWP3cW3jYS1119CX_6A3eS6p7XyihKCUCdkoWChXcq3FB3MocW_L0QA1p7TNkrZpoZpT2ua2aZ7fOc_93g-_Fb_ibQBbgNpaaevLX6P_4_piEQWbjd2WWM31F0ZB0nba7-L8JxwCvpk</recordid><startdate>20150401</startdate><enddate>20150401</enddate><creator>Hong, Seung-Hye</creator><creator>Ngo, Ho-Phuong-Thuy</creator><creator>Kang, Lin-Woo</creator><creator>Oh, Deok-Kun</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20150401</creationdate><title>Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol</title><author>Hong, Seung-Hye ; Ngo, Ho-Phuong-Thuy ; Kang, Lin-Woo ; Oh, Deok-Kun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-115c27d75e744c5093f1630567cb85c17ffb9da61f7a2bb5e54c299ca76512793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Alcanivoraceae - enzymology</topic><topic>Alcanivoraceae - genetics</topic><topic>Alcanivoraceae - isolation & purification</topic><topic>Alcohol dehydrogenase</topic><topic>Alcohol Dehydrogenase - chemistry</topic><topic>Alcohol Dehydrogenase - genetics</topic><topic>Alcohol Dehydrogenase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Applied Microbiology</topic><topic>Bacteria</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Coenzymes - metabolism</topic><topic>Conversion</topic><topic>Dehydrogenase</topic><topic>Dermatology</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Hydrogen-Ion Concentration</topic><topic>hydroquinone</topic><topic>Hydroquinones - metabolism</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>methanol</topic><topic>Methanol - metabolism</topic><topic>Methyl alcohol</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>NAD (coenzyme)</topic><topic>NAD - metabolism</topic><topic>NADH</topic><topic>Optimization</topic><topic>Original Research Paper</topic><topic>Phylogeny</topic><topic>Protein Multimerization</topic><topic>Recombinant</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Skin diseases</topic><topic>Temperature</topic><topic>Vitamin A - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hong, Seung-Hye</creatorcontrib><creatorcontrib>Ngo, Ho-Phuong-Thuy</creatorcontrib><creatorcontrib>Kang, Lin-Woo</creatorcontrib><creatorcontrib>Oh, Deok-Kun</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hong, Seung-Hye</au><au>Ngo, Ho-Phuong-Thuy</au><au>Kang, Lin-Woo</au><au>Oh, Deok-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2015-04-01</date><risdate>2015</risdate><volume>37</volume><issue>4</issue><spage>849</spage><epage>856</epage><pages>849-856</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>A recombinant alcohol dehydrogenase (ADH) from Kangiella koreensis was purified as a 40 kDa dimer with a specific activity of 21.3 nmol min⁻¹ mg⁻¹, a Kₘof 1.8 μM, and a kcₐₜof 1.7 min⁻¹for all-trans-retinal using NADH as cofactor. The enzyme showed activity for all-trans-retinol using NAD ⁺ as a cofactor. The reaction conditions for all-trans-retinol production were optimal at pH 6.5 and 60 °C, 2 g enzyme l⁻¹, and 2,200 mg all-trans-retinal l⁻¹in the presence of 5 % (v/v) methanol, 1 % (w/v) hydroquinone, and 10 mM NADH. Under optimized conditions, the ADH produced 600 mg all-trans-retinol l⁻¹after 3 h, with a conversion yield of 27.3 % (w/w) and a productivity of 200 mg l⁻¹ h⁻¹. This is the first report of the characterization of a bacterial ADH for all-trans-retinal and the biotechnological production of all-trans-retinol using ADH.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>25481533</pmid><doi>10.1007/s10529-014-1740-x</doi><tpages>8</tpages></addata></record> |
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| subjects | Alcanivoraceae - enzymology Alcanivoraceae - genetics Alcanivoraceae - isolation & purification Alcohol dehydrogenase Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Amino Acid Sequence Applied Microbiology Bacteria Biochemistry Biomedical and Life Sciences Biotechnology Coenzymes - metabolism Conversion Dehydrogenase Dermatology Enzyme Stability Enzymes Hydrogen-Ion Concentration hydroquinone Hydroquinones - metabolism Kinetics Life Sciences methanol Methanol - metabolism Methyl alcohol Microbiology Molecular Sequence Data Molecular Weight NAD (coenzyme) NAD - metabolism NADH Optimization Original Research Paper Phylogeny Protein Multimerization Recombinant Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Homology, Amino Acid Skin diseases Temperature Vitamin A - metabolism |
| title | Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol |
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