Glycosylation and pH stability of penicillin G acylase from Providencia rettgeri produced in Pichia pastoris
Senerovic, L., Max Plank Institute for Infectious Biology, Berlin (Germany) | Stankovic, N., Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia) | Ljubijankic, G., Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia) | Vasiljevic, B., Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia)
Penicillin G acylase (PAC) is one of the most widely used enzymes in industrail synthesis of semi-synthetic antibiotics. The Providencia rettgeri pac gene was expressed to a level of 2.7 U/ml using the Pichia pastoris expression system. The recombinant enzyme was purified and its glycosylation status was determined. It was found that both subunits (alfa and beta) of the enzyme were N-glycosylated, while the beta-subunit also contained O-glycans. It was also observed that rPACP.rett. was stable in a wide range of pH, which, in addition to the previously proved high thermostability, makes it an attractive biocatalyst from an industrial point of view.
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