Isolation of α‐Terpineol Dehydratase from Pseudomonas gladioli

An enzyme which converts the citrus by‐product limonene to α‐terpineol was purified 13‐fold. After cell disruption of P. gladioli, α‐terpineol dehydratase (α‐TD) remained associated with a heterogeneous group of particulate material. α‐TD was partially solubilized by extraction with 10 mM HEPES buffer, pH 7.0 containing 2.0% (w/v) Triton X‐100 and 0.5M sodium trichloroacetate. Two soluble forms existed in 1.0% (w/v) Triton X‐100 with apparent molecular weights of 94,500 and 206,500 daltons.