<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Prem S</submitter><funding>Bundesministerium für Bildung und Forschung</funding><funding>Freie Universität Berlin</funding><pagination>58</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8994360</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(1)</volume><pubmed_abstract>Fatty acid hydratases are unique to microorganisms. Their native function is the oxidation of unsaturated C-C bonds to enable detoxification of environmental toxins. Within this enzyme family, the oleate hydratases (Ohys), which catalyze the hydroxylation of oleic acid to 10-(R)-hydroxy stearic acid (10-HSA) have recently gained particular industrial interest. 10-HSA is considered to be a replacement for 12-(R)-hydroxy stearic acid (12-HSA), which has a broad application in the chemical and pharmaceutical industry. As 12-HSA is obtained through an energy consuming synthesis process, the biotechnological route for sustainable 10-HSA production is of significant industrial interest. All Ohys identified to date have a non-redox active FAD bound in their active site. Ohys can be divided in sev</pubmed_abstract><journal>Microbial cell factories</journal><pubmed_title>Towards an understanding of oleate hydratases and their application in industrial processes.</pubmed_title><pmcid>PMC8994360</pmcid><funding_grant_id>03SF0577A</funding_grant_id><funding_grant_id>031B0853</funding_grant_id><pubmed_authors>Helmer CPO</pubmed_authors><pubmed_authors>Dimos N</pubmed_authors><pubmed_authors>Bruck T</pubmed_authors><pubmed_authors>Prem S</pubmed_authors><pubmed_authors>Garbe D</pubmed_authors><pubmed_authors>Loll B</pubmed_authors><pubmed_authors>Himpich S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Towards an understanding of oleate hydratases and their application in industrial processes.</name><description>Fatty acid hydratases are unique to microorganisms. Their native function is the oxidation of unsaturated C-C bonds to enable detoxification of environmental toxins. Within this enzyme family, the oleate hydratases (Ohys), which catalyze the hydroxylation of oleic acid to 10-(R)-hydroxy stearic acid (10-HSA) have recently gained particular industrial interest. 10-HSA is considered to be a replacement for 12-(R)-hydroxy stearic acid (12-HSA), which has a broad application in the chemical and pharmaceutical industry. As 12-HSA is obtained through an energy consuming synthesis process, the biotechnological route for sustainable 10-HSA production is of significant industrial interest. All Ohys identified to date have a non-redox active FAD bound in their active site. Ohys can be divided in sev</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Apr</publication><modification>2026-05-31T21:04:25.252Z</modification><creation>2025-04-04T19:30:29.025Z</creation></dates><accession>S-EPMC8994360</accession><cross_references><pubmed>35397585</pubmed><doi>10.1186/s12934-022-01777-6</doi></cross_references></HashMap>