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

  • Junmei DingEmail author
  • Yang Zhou
  • Hujie Zhu
  • Ming Deng
  • Liangchuan Long
  • Yunjuan Yang
  • Qian Wu
  • Zunxi HuangEmail author
Original Research Paper



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


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.


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


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



This work was supported by grants from the National Natural Science Foundation of China (Grant Nos. 31600083, 31460022), the Natural Science Foundation of Yunnan Province (Grant No. 2016FB036), the National Key Research and Development Program of China (Grant No. 2017YFB0308401), and the Reserve Talents Project for Young and Middle-Aged Academic and Technical Leaders of Yunnan Province (Grant No. 2018HB059).

Supporting information

Supplementary Table 1—Primers used for site-directed mutagenesis in this study.

Supplementary Fig. 1—Molecular model of the AesZY structure.

Supplementary Fig. 2—Site-directed mutagenesis of the putative catalytic triads.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

10529_2019_2709_MOESM1_ESM.docx (1.2 mb)
Supplementary material 1 (DOCX 1231 kb)


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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of EducationYunnan Normal UniversityKunmingChina
  2. 2.Key Laboratory of Yunnan for Biomass Energy and Biotechnology of EnvironmentKunmingChina
  3. 3.Key Laboratory of Enzyme EngineeringYunnan Normal UniversityKunmingChina

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