Purification and characterization of acetyl esterase from Candida guilliermondii.
An extracellular acetyl esterase (EC 3.1.1.6) from Candida guilliermondii NRRL Y-17257 was purified to homogeneity by acetone precipitation and QAE sepharose anion-exchange chromatography. The enzyme was a monomer with an apparent molecular weight of 67 kDa and a pI of 7.6. It had maximum activity at pH 7.5 and at 50-60 degrees C. It was relatively stable over a pH range of 5.8-8.0 and exhibited thermal stability up to 60 degrees C. The Km and Vmax values on alpha-naphthylacetate were 2.63 mM and 213.3 micromol alpha- naphthol min-1 mg-1 protein, respectively.
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Department of Food Science and Technology, Cornell University, Geneva, New York 14456, USA. pb27@cornell.edu
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D000115:Acetylesterase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D002175:Candida / Q000201:enzymology* / Q000254:growth & development; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D013696:Temperature; D014990:Xylans / Q000378:metabolism
D014990:Xylans; D000115:Acetylesterase