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Expression and characterization of a thermostable penicillin G acylase from an environmental metagenomic library
Authors:Qian Zhang  Hui Xu  Jing Zhao  Runying Zeng
Affiliation:1. Department of Civil and Environmental Engineering, University of Hawaii at Manoa, Honolulu, HI, USA
2. Key Laboratory of Marine Genetic Resource-State Key Laboratory Breeding Base, Third Institute of Oceanography, SOA, Daxue road 178#, Xiamen, 361005, China
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.
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