ReviewMicrobial cell factories2022
Towards an understanding of oleate hydratases and their application in industrial processes.
Review in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.Microbial cell factories · 2026Article
- A Comparative Biochemical Study of Oleate Hydratases.Chembiochem : a European journal of chemical biology · 2026Article
- Article
- A Comprehensive Review on Medium- and Long-Chain Fatty Acid-Derived Metabolites: From Energy Sources to Metabolic Signals.Metabolites · 2026Review
- A Thermostable Fatty Acid Hydratase from Marinitoga Piezophila with Low Temperature Optimum and Broad Product Scope.Chembiochem : a European journal of chemical biology · 2025Article
- Valorization of Oil Cakes in Two-Pot Lactone Biosynthesis Process.Foods (Basel, Switzerland) · 2025Article
- Article
- Influence of Salinity on the Extracellular Enzymatic Activities of Marine Pelagic Fungi.Journal of fungi (Basel, Switzerland) · 2024Article
- Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Dissecting the biophysical mechanisms of oleate hydratase association with membranes.Frontiers in molecular biosciences · 2024Article
- Mastering targeted genome engineering of GC-rich oleaginous yeast for tailored plant oil alternatives for the food and chemical sector.Microbial cell factories · 2023Article
- Chiral Alcohols from Alkenes and Water: Directed Evolution of a Styrene Hydratase.Angewandte Chemie (International ed. in English) · 2023Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
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 several subfamilies, that differ in their oligomerization state and the decoration with amino acids in their active sites. The latter observation indicates a different reaction mechanism across those subfamilies. Despite intensive biotechnological, biochemical and structural investigations, surprising little is known about substrate binding and the reaction mechanism of this enzyme family. This review, summarizes our current understanding of Ohys with a focus on sustainable biotransformation.
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