Towards an understanding of oleate hydratases and their application in industrial processes

• Published in: Microbial cell factories Vol. 21; no. 1; p. 58
• Main Authors: Prem, Sophia, Helmer, Carl P O, Dimos, Nicole, Himpich, Stephanie, Brück, Thomas, Garbe, Daniel, Loll, Bernhard
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 09.04.2022; BioMed Central; BMC
• Subjects: Amino acids; Bacteria; Binding sites; Biocatalysis; Biocatalysts; Biodegradation, Environmental; Bioeconomics; Biotechnology; Biotransformation; Catalysis; Catalytic Domain; Covalent bonds; Detoxification; Enzymes; Fatty acids; Gram-positive bacteria; Green chemistry; Green technology; Hydro-Lyases - chemistry; Hydro-Lyases - metabolism; Hydrogenation; Hydroxylation; Industrial applications; Industrial biotechnology; Methods; Microorganisms; Oleate hydratase; Oleic acid; Oleic Acid - metabolism; Oligomerization; Oxidation; Oxidation-Reduction; Pharmaceutical industry; Prevention; Protein engineering; Proteins; Reaction mechanisms; Review; Risk factors; Skin; Staphylococcus aureus infections; Stearic acid; Stearic Acids; Substrates; Toxins; Whole cell and enzymatic oleic acid transformation; Germany; Protein engineering; Structure–function relation; Biocatalysis; Whole cell and enzymatic oleic acid transformation; Green chemistry; Oleate hydratase; Industrial biotechnology; Bioeconomy
• ISSN: 1475-2859; 1475-2859
• DOI: 10.1186/s12934-022-01777-6

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.