Hydrogen‐Borrowing Alcohol Bioamination with Coimmobilized Dehydrogenases
The amination of alcohols is an important transformation in chemistry. The redox‐neutral (i.e., hydrogen‐borrowing) asymmetric amination of alcohols is enabled by the combination of an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH). In this work, we enhanced the efficiency of hydroge...
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| Veröffentlicht in: | ChemCatChem 2018-02, Vol.10 (4), p.731-735 |
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| creator | Böhmer, Wesley Knaus, Tanja Mutti, Francesco G. |
| description | The amination of alcohols is an important transformation in chemistry. The redox‐neutral (i.e., hydrogen‐borrowing) asymmetric amination of alcohols is enabled by the combination of an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH). In this work, we enhanced the efficiency of hydrogen‐borrowing biocatalytic amination by co‐immobilizing both dehydrogenases on controlled porosity glass FeIII ion‐affinity beads. The recyclability of the dual‐enzyme system was demonstrated (5 cycles) with total turnover numbers of >4000 and >1000 for ADH and AmDH, respectively. A set of (S)‐configured alcohol substrates was aminated with up to 95 % conversion and >99 % ee (R). Preparative‐scale amination of (S)‐phenylpropan‐2‐ol resulted in 90 % conversion and 80 % yield of the product in 24 h.
Something borrowed: We co‐immobilize an alcohol dehydrogenase (ADH) and an amine dehydrogenase (AmDH) on controlled porosity glass FeIII affinity beads to perform the hydrogen‐borrowing amination of (S)‐configured alcohols with up to 95 % conversion, >99 % ee. Recyclability of the dual‐enzyme system is demonstrated, whereas the total turnover numbers are >4000 and >1000 for ADH and AmDH, respectively. |
| doi_str_mv | 10.1002/cctc.201701366 |
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Something borrowed: We co‐immobilize an alcohol dehydrogenase (ADH) and an amine dehydrogenase (AmDH) on controlled porosity glass FeIII affinity beads to perform the hydrogen‐borrowing amination of (S)‐configured alcohols with up to 95 % conversion, >99 % ee. Recyclability of the dual‐enzyme system is demonstrated, whereas the total turnover numbers are >4000 and >1000 for ADH and AmDH, respectively.</description><identifier>ISSN: 1867-3880</identifier><identifier>EISSN: 1867-3899</identifier><identifier>DOI: 10.1002/cctc.201701366</identifier><identifier>PMID: 29515675</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Alcohol ; Alcohol dehydrogenase ; Alcohols ; amination ; Beads ; biocatalysis ; Communication ; Communications ; Conversion ; Dehydrogenases ; enzyme immobilization ; Hydrogen ; hydrogen borrowing ; Porosity ; Recyclability ; Substrates</subject><ispartof>ChemCatChem, 2018-02, Vol.10 (4), p.731-735</ispartof><rights>2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.</rights><rights>2018 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4686-7fd9e3b93c7f23c1d5b1234654622ea42d999058ac58a6368e67d4259028d1dc3</citedby><cites>FETCH-LOGICAL-c4686-7fd9e3b93c7f23c1d5b1234654622ea42d999058ac58a6368e67d4259028d1dc3</cites><orcidid>0000-0002-6771-5102 ; 0000-0003-3641-6166 ; 0000-0001-9942-9226</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcctc.201701366$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcctc.201701366$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29515675$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Böhmer, Wesley</creatorcontrib><creatorcontrib>Knaus, Tanja</creatorcontrib><creatorcontrib>Mutti, Francesco G.</creatorcontrib><title>Hydrogen‐Borrowing Alcohol Bioamination with Coimmobilized Dehydrogenases</title><title>ChemCatChem</title><addtitle>ChemCatChem</addtitle><description>The amination of alcohols is an important transformation in chemistry. The redox‐neutral (i.e., hydrogen‐borrowing) asymmetric amination of alcohols is enabled by the combination of an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH). In this work, we enhanced the efficiency of hydrogen‐borrowing biocatalytic amination by co‐immobilizing both dehydrogenases on controlled porosity glass FeIII ion‐affinity beads. The recyclability of the dual‐enzyme system was demonstrated (5 cycles) with total turnover numbers of >4000 and >1000 for ADH and AmDH, respectively. A set of (S)‐configured alcohol substrates was aminated with up to 95 % conversion and >99 % ee (R). Preparative‐scale amination of (S)‐phenylpropan‐2‐ol resulted in 90 % conversion and 80 % yield of the product in 24 h.
Something borrowed: We co‐immobilize an alcohol dehydrogenase (ADH) and an amine dehydrogenase (AmDH) on controlled porosity glass FeIII affinity beads to perform the hydrogen‐borrowing amination of (S)‐configured alcohols with up to 95 % conversion, >99 % ee. Recyclability of the dual‐enzyme system is demonstrated, whereas the total turnover numbers are >4000 and >1000 for ADH and AmDH, respectively.</description><subject>Alcohol</subject><subject>Alcohol dehydrogenase</subject><subject>Alcohols</subject><subject>amination</subject><subject>Beads</subject><subject>biocatalysis</subject><subject>Communication</subject><subject>Communications</subject><subject>Conversion</subject><subject>Dehydrogenases</subject><subject>enzyme immobilization</subject><subject>Hydrogen</subject><subject>hydrogen borrowing</subject><subject>Porosity</subject><subject>Recyclability</subject><subject>Substrates</subject><issn>1867-3880</issn><issn>1867-3899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNqFkctOAyEUhonReKluXZpJ3Lhp5TLAsDGx4zWauNE1oUBbzMygMLWpKx_BZ_RJpGmtl40LAgnf-XLO-QHYR7CHIMTHWre6hyHiEBHG1sA2KhjvkkKI9dW7gFtgJ8ZHCJkgnG6CLSwooozTbXBzNTPBj2zz8fbe9yH4qWtG2Wml_dhXWd95VbtGtc432dS146z0rq79wFXu1ZrszI6X5SrauAs2hqqKdm95d8DDxfl9edW9vbu8Lk9vuzpnBevyoRGWDATRfIiJRoYOECY5oznD2KocGyEEpIXS6TDCCsu4yTEVEBcGGU064GThfZoMamu0bdqgKvkUXK3CTHrl5O-fxo3lyL9IWpD5npLgaCkI_nliYytrF7WtKtVYP4ky7RMjlAvEE3r4B330k9Ck8RIFGc8FTMYO6C0oHXyMwQ5XzSAo5znJeU5ylVMqOPg5wgr_CiYBYgFMXWVn_-hkWd6X3_JPqx6gtA</recordid><startdate>20180221</startdate><enddate>20180221</enddate><creator>Böhmer, Wesley</creator><creator>Knaus, Tanja</creator><creator>Mutti, Francesco G.</creator><general>Wiley Subscription Services, Inc</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-6771-5102</orcidid><orcidid>https://orcid.org/0000-0003-3641-6166</orcidid><orcidid>https://orcid.org/0000-0001-9942-9226</orcidid></search><sort><creationdate>20180221</creationdate><title>Hydrogen‐Borrowing Alcohol Bioamination with Coimmobilized Dehydrogenases</title><author>Böhmer, Wesley ; Knaus, Tanja ; Mutti, Francesco G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4686-7fd9e3b93c7f23c1d5b1234654622ea42d999058ac58a6368e67d4259028d1dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Alcohol</topic><topic>Alcohol dehydrogenase</topic><topic>Alcohols</topic><topic>amination</topic><topic>Beads</topic><topic>biocatalysis</topic><topic>Communication</topic><topic>Communications</topic><topic>Conversion</topic><topic>Dehydrogenases</topic><topic>enzyme immobilization</topic><topic>Hydrogen</topic><topic>hydrogen borrowing</topic><topic>Porosity</topic><topic>Recyclability</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Böhmer, Wesley</creatorcontrib><creatorcontrib>Knaus, Tanja</creatorcontrib><creatorcontrib>Mutti, Francesco G.</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Wiley Online Library (Open Access Collection)</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>ChemCatChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Böhmer, Wesley</au><au>Knaus, Tanja</au><au>Mutti, Francesco G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydrogen‐Borrowing Alcohol Bioamination with Coimmobilized Dehydrogenases</atitle><jtitle>ChemCatChem</jtitle><addtitle>ChemCatChem</addtitle><date>2018-02-21</date><risdate>2018</risdate><volume>10</volume><issue>4</issue><spage>731</spage><epage>735</epage><pages>731-735</pages><issn>1867-3880</issn><eissn>1867-3899</eissn><abstract>The amination of alcohols is an important transformation in chemistry. The redox‐neutral (i.e., hydrogen‐borrowing) asymmetric amination of alcohols is enabled by the combination of an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH). In this work, we enhanced the efficiency of hydrogen‐borrowing biocatalytic amination by co‐immobilizing both dehydrogenases on controlled porosity glass FeIII ion‐affinity beads. The recyclability of the dual‐enzyme system was demonstrated (5 cycles) with total turnover numbers of >4000 and >1000 for ADH and AmDH, respectively. A set of (S)‐configured alcohol substrates was aminated with up to 95 % conversion and >99 % ee (R). Preparative‐scale amination of (S)‐phenylpropan‐2‐ol resulted in 90 % conversion and 80 % yield of the product in 24 h.
Something borrowed: We co‐immobilize an alcohol dehydrogenase (ADH) and an amine dehydrogenase (AmDH) on controlled porosity glass FeIII affinity beads to perform the hydrogen‐borrowing amination of (S)‐configured alcohols with up to 95 % conversion, >99 % ee. Recyclability of the dual‐enzyme system is demonstrated, whereas the total turnover numbers are >4000 and >1000 for ADH and AmDH, respectively.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29515675</pmid><doi>10.1002/cctc.201701366</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-6771-5102</orcidid><orcidid>https://orcid.org/0000-0003-3641-6166</orcidid><orcidid>https://orcid.org/0000-0001-9942-9226</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alcohol Alcohol dehydrogenase Alcohols amination Beads biocatalysis Communication Communications Conversion Dehydrogenases enzyme immobilization Hydrogen hydrogen borrowing Porosity Recyclability Substrates |
| title | Hydrogen‐Borrowing Alcohol Bioamination with Coimmobilized Dehydrogenases |
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