Biocatalytic Production of Perillyl Alcohol from Limonene by Using a Novel <i>Mycobacterium</i> sp. Cytochrome P450 Alkane Hydroxylase Expressed in <i>Pseudomonas putida</i>

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<jats:title>ABSTRACT</jats:title> <jats:p> A number of oxygenated monoterpenes present at low concentrations in plant oils have anticarcinogenic properties. One of the most promising compounds in this respect is (−)-perillyl alcohol. Since this natural product is present only at low levels in a few plant oils, an alternative, synthetic source is desirable. Screening of 1,800 bacterial strains showed that many alkane degraders were able to specifically hydroxylate <jats:sc>l</jats:sc> -limonene in the 7 position to produce enantiopure (−)-perillyl alcohol. The oxygenase responsible for this was purified from the best-performing wild-type strain, <jats:italic>Mycobacterium</jats:italic> sp. strain HXN-1500. By using N-terminal sequence information, a 6.2-kb ApaI fragment was cloned, which encoded a cytochrome P450, a ferredoxin, and a ferredoxin reductase. The three genes were successfully coexpressed in <jats:italic>Pseudomonas putida</jats:italic> by using the broad-host-range vector pCom8, and the recombinant converted limonene to perillyl alcohol with a specific activity of 3 U/g (dry weight) of cells. The construct was subsequently used in a 2-liter bioreactor to produce perillyl alcohol on a scale of several grams. </jats:p>

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