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 language | English (US) |
|---|---|
| Pages (from-to) | 617-625 |
| Number of pages | 9 |
| Journal | Biotechnology Letters |
| Volume | 36 |
| Issue number | 3 |
| DOIs | |
| State | Published - 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).
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 9 Industry, Innovation, and Infrastructure
Keywords
- Characterization
- Gene expression
- Metagenomic library
- Penicillin G acylase
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