Purification and characterization of acetyl esterase from Candida guilliermondii

Basaran P., Hang Y.

Letters in Applied Microbiology, cilt.30, sa.2, ss.167-171, 2000 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 30 Sayı: 2
  • Basım Tarihi: 2000
  • Doi Numarası: 10.1046/j.1472-765x.2000.00681.x
  • Dergi Adı: Letters in Applied Microbiology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.167-171
  • İstanbul Teknik Üniversitesi Adresli: Hayır

Özet

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.