Identification and characterization of an acetyl esterase from Paenibacillus sp. XW-6-66 and its novel function in 7-aminocephalosporanic acid deacetylation

Biotechnol Lett. 2019 Sep;41(8-9):1059-1065. doi: 10.1007/s10529-019-02709-y. Epub 2019 Jul 13.

Abstract

Objectives: To obtain a new acetyl esterase from Paenibacillus sp. XW-6-66 and apply the enzyme to 7-aminocephalosporanic acid (7-ACA) deacetylation.

Results: The acetyl esterase AesZY was identified from Paenibacillus sp. XW-6-66, and its enzymatic properties were investigated. With the putative catalytic triad Ser114-Asp203-His235, AesZY belongs to the Acetyl esterase (Aes) family which is included in the α/β hydrolase superfamily and contains the consensus Gly-X-Ser-X-Gly motif. The maximum activity of AesZY was detected at pH 8.0 and 40 °C. AesZY was stable at different pH values ranging from 5.0 to 12.0, and was tolerant to several metal ions. Furthermore, the deacetylation activity of AesZY toward 7-ACA was approximately 7.5 U/mg, and the Kcat/Km value was 2.04 s-1 mM-1.

Conclusions: Our results demonstrate the characterization of a new acetyl esterase belonging to the Aes family with potential biotechnological applications.

Keywords: 7-Aminocephalosporanic acid; Aes superfamily; Deacetylation; Paenibacillus sp. XW-6-66.

MeSH terms

  • Acetylesterase / genetics
  • Acetylesterase / isolation & purification
  • Acetylesterase / metabolism*
  • Biotransformation
  • Cephalosporins / metabolism*
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Kinetics
  • Paenibacillus / enzymology*
  • Paenibacillus / genetics
  • Temperature

Substances

  • Cephalosporins
  • 7-aminocephalosporanic acid
  • Acetylesterase