Expression and characterization of a thermostable penicillin G acylase from an environmental metagenomic library

Qian Zhang, Hui Xu, Jing Zhao, Runying Zeng

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7 Scopus citations

Abstract

One clone (ACPGA001) exhibiting penicillin G acylase (PGA) activity was screened from a metagenomic library by using a medium containing penicillin G. A novel PGA gene from the inserted fragment of ACPGA001 was obtained by sequencing. The amino acid sequence of ACPGA001 PGA exhibited <33 % similarity to PGAs retrieved from GenBank. This gene was expressed in Escherichia coli M15 and the recombinant protein was purified and characterized. The ACPGA001 PGA exhibited a maximum activity at 60 °C and showed high activity at pH 4-10 with an optimum pH of 8.0. This enzyme was stable at 40 °C for 70 min with a half-life of 60 min at 55 °C. These beneficial characteristics of ACPGA001 PGA provide some advantages for the potential application of ACPGA001 PGA in industry.

Original languageEnglish (US)
Pages (from-to)617-625
Number of pages9
JournalBiotechnology Letters
Volume36
Issue number3
DOIs
StatePublished - Mar 2014

Bibliographical note

Funding Information:
Acknowledgments This work was financially supported by Hi-Tech Research and Development Program of China (863 program of China; 2012AA092103), China Ocean Mineral Resources R&D Association (DY125-15-T-06) and Marine Scientific Research Special Foundation for Public Sector Program (201005032).

Keywords

  • Characterization
  • Gene expression
  • Metagenomic library
  • Penicillin G acylase

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