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Purification and characterization of acetyl esterase from Candida guilliermondii

Basaran, P.; Hang, Y.D.

Letters in Applied Microbiology 30(2): 167-171

2000


ISSN/ISBN: 0266-8254
PMID: 10736022
DOI: 10.1046/j.1472-765x.2000.00681.x
Accession: 011226534

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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