Purification and characterization of acetyl esterase from Candida guilliermondii

P. Basaran; Y. D. Hang

doi:10.1046/j.1472-765x.2000.00681.x

Purification and characterization of acetyl esterase from Candida guilliermondii

P. Basaran^*, Y. D. Hang

^*Corresponding author for this work

Cornell University

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

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°C. It was relatively stable over a pH range of 5.8-8.0 and exhibited thermal stability up to 60°C. The K(m) and V(max) values on α-naphthylacetate were 2.63 mM and 213.3 μmol α-naphthol min^-1 mg^-1 protein, respectively.

Original language	English
Pages (from-to)	167-171
Number of pages	5
Journal	Letters in Applied Microbiology
Volume	30
Issue number	2
DOIs	https://doi.org/10.1046/j.1472-765x.2000.00681.x
Publication status	Published - 2000
Externally published	Yes

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abstract = "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°C. It was relatively stable over a pH range of 5.8-8.0 and exhibited thermal stability up to 60°C. The K(m) and V(max) values on α-naphthylacetate were 2.63 mM and 213.3 μmol α-naphthol min-1 mg-1 protein, respectively.",

author = "P. Basaran and Hang, \{Y. D.\}",

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doi = "10.1046/j.1472-765x.2000.00681.x",

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AU - Basaran, P.

AU - Hang, Y. D.

PY - 2000

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N2 - 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°C. It was relatively stable over a pH range of 5.8-8.0 and exhibited thermal stability up to 60°C. The K(m) and V(max) values on α-naphthylacetate were 2.63 mM and 213.3 μmol α-naphthol min-1 mg-1 protein, respectively.

AB - 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°C. It was relatively stable over a pH range of 5.8-8.0 and exhibited thermal stability up to 60°C. The K(m) and V(max) values on α-naphthylacetate were 2.63 mM and 213.3 μmol α-naphthol min-1 mg-1 protein, respectively.

UR - https://www.scopus.com/pages/publications/0034049234

U2 - 10.1046/j.1472-765x.2000.00681.x

DO - 10.1046/j.1472-765x.2000.00681.x

M3 - Article

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SN - 0266-8254

VL - 30

SP - 167

EP - 171

JO - Letters in Applied Microbiology

JF - Letters in Applied Microbiology

IS - 2

ER -

Purification and characterization of acetyl esterase from Candida guilliermondii

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