Production of 10-hydroxystearic acid from oleic acid by whole cells of recombinant Escherichia coli containing oleate hydratase from Stenotrophomonas maltophilia

A putative fatty acid hydratase from Stenotrophomonas maltophilia was cloned and expressed in Escherichia coli. The recombinant enzyme showed the highest hydration activity for oleic acid among the fatty acids tested, indicating that the enzyme is an oleate hydratase. The optimal conditions for the production of 10-hydroxystearic acid from oleic acid using whole cells of recombinant E. coli containing the oleate hydratase were pH 6.5, 35 °C, 0.05% (w/v) Tween 40, 10 g l−1 cells, and 50 g l−1 oleic acid. Under these conditions, whole recombinant cells produced 49 g l−1 10-hydroxystearic acid for 4 h, with a conversion yield of 98% (w/w), a volumetric productivity of 12.3 g l−1 h−1, and a specific productivity of 1.23 g g-cells−1 h−1, which were 18%, 2.5-, and 2.5-fold higher than those of whole wild-type S. maltophilia cells, respectively. This is the first report of 10-hydroxystearic acid production using recombinant cells and the concentration and productivity are the highest reported thus far among cells.

► Oleate hydratase from Stenotrophomonas maltophilia is characterized.
► Recombinant E. coli containing the oleate hydratase produced 10-hydroxystearic acid.
► This is the first report of 10-hydroxystearic acid production by recombinant cells.
► The concentration and productivity of the product are the highest reported thus far.