Isolation and partial characterization of an esterase (EC 3.1.1.1) from a Debaryomyces hansenii strain

Abstract

Esterase extracted from a strain of Debaryomyces hansenii isolated from the surface of Roquefort cheese was purified 224-fold by ion-exchange chromatography on a Q Sepharose Fast Flow column and gel filtration on a Sephacryl HR S200 column. It was identified as a monomeric enzyme of 80 kDa. Tributyrin and ethyl butyrate were hydrolysed with maximum activity at pH 8 and 35°C. Activity on tributyrin was tested in the presence of several metal ions and chemical effectors. The esterase hydrolysed the methyl and ethyl esters of short-chain fatty acids (C2 to C5) very well and esters of longer-chain fatty acids (C6 to C14) moderatly. Aliphatic and aromatic acetate esters were also hydrolysed.