Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: Partial purification and preliminary biochemical characterisation

A method to purify these enzymes from postincubates of T. thermophilus HB27 was developed following three steps: sodium cholate treatment, ethanol/ether precipitation and hydrophobic chromatography. In this way, an enzyme solution was obtained that contained the identified esterases/lipases. The partially purified enzymes showed an optimum of activity for the hydrolysis of p-nitrophenyl laurate at alkaline pH values and 80 °C, a high thermal stability and were very stable in the presence of high concentrations of isopropanol.