<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chen Y</submitter><funding>Shanghai Municipal Education Commission</funding><funding>Shanghai Institute of Technology</funding><pagination>2325-2331</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9059822</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>9(4)</volume><pubmed_abstract>The production of (&lt;i>S&lt;/i>)-&lt;i>N&lt;/i>-boc-3-hydroxy piperidine (NBHP) &lt;i>via&lt;/i> asymmetric bioreduction of 1-boc-3-piperidinone with reductase is impeded by the need for expensive coenzymes NAD(P)H. In order to regenerate the coenzyme &lt;i>in situ&lt;/i>, the gene of alcohol dehydrogenase from &lt;i>Thermoanaerobacter brockii&lt;/i> and glucose dehydrogenase from &lt;i>Bacillus subtilis&lt;/i> were ligated into the multiple cloning sites of pRSFDuet-1 plasmid to construct the recombinant &lt;i>Escherichia&lt;/i> BL21 (DE3) that co-expressing alcohol dehydrogenase and glucose dehydrogenase. Different culture conditions including the medium composition, inducer and pH &lt;i>etc&lt;/i> were systematically investigated to improve the enzyme production. The enzyme activity was increased more than 11-fold under optimal cul</pubmed_abstract><journal>RSC advances</journal><pubmed_title>Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant &lt;i>E. coli&lt;/i> co-expressing alcohol dehydrogenase and glucose dehydrogenase.</pubmed_title><pmcid>PMC9059822</pmcid><funding_grant_id>No. ZZyyx15011</funding_grant_id><funding_grant_id>No. YJ2015-36</funding_grant_id><pubmed_authors>Ma B</pubmed_authors><pubmed_authors>Cao S</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Wu X</pubmed_authors><pubmed_authors>Xu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant &lt;i>E. coli&lt;/i> co-expressing alcohol dehydrogenase and glucose dehydrogenase.</name><description>The production of (&lt;i>S&lt;/i>)-&lt;i>N&lt;/i>-boc-3-hydroxy piperidine (NBHP) &lt;i>via&lt;/i> asymmetric bioreduction of 1-boc-3-piperidinone with reductase is impeded by the need for expensive coenzymes NAD(P)H. In order to regenerate the coenzyme &lt;i>in situ&lt;/i>, the gene of alcohol dehydrogenase from &lt;i>Thermoanaerobacter brockii&lt;/i> and glucose dehydrogenase from &lt;i>Bacillus subtilis&lt;/i> were ligated into the multiple cloning sites of pRSFDuet-1 plasmid to construct the recombinant &lt;i>Escherichia&lt;/i> BL21 (DE3) that co-expressing alcohol dehydrogenase and glucose dehydrogenase. Different culture conditions including the medium composition, inducer and pH &lt;i>etc&lt;/i> were systematically investigated to improve the enzyme production. The enzyme activity was increased more than 11-fold under optimal cul</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Jan</publication><modification>2025-05-18T12:06:57.788Z</modification><creation>2025-05-18T12:06:57.788Z</creation></dates><accession>S-EPMC9059822</accession><cross_references><pubmed>35516114</pubmed><doi>10.1039/c8ra08100j</doi></cross_references></HashMap>