Abstract
AbstractOleate hydratases convert oleic acid into 10‐hydroxy stearic acid, a valuable fine chemical, useful in lubricant and surfactant formulations. They are of large interest due to their high expression rates and solubility, however, they differ drastically by their overall stability and pH‐ and temperature ranges. To expand their portfolio, another oleate hydratase named OhyPp (originating from Pediococcus parvulus) was characterized. It is a close relative of the well‐known oleate hydratase OhyRe from Rhodococcus erythropolis. OhyPp is only the second member of the monomeric oleate hydratase family with some surprising catalytic features. A distinct characteristic is OhyPp's higher affinity towards FAD compared to OhyRe's helping to understand and improve FAD binding in the future, which is a current drawback for the industrial application of oleate hydratases.
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