Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris-Reference-Cited by-同舟云学术

Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris

Published:2009 Issue:4 Volume:61 Page:581-586
ISSN:0354-4664
Container-title:Archives of Biological Sciences
language:en
Short-container-title:ARCH BIOL SCI BELGRA

Author:

Senerovic Lidija¹,Stankovic Nad²,Ljubijankic G.²,Vasiljevic Branka²^ORCID

Affiliation:

1. Institut za molekularnu genetiku i genetičko inženjerstvo, Beograd + Max Planck Institute for Infection Biology, Berlin, Nemačka

2. Institut za molekularnu genetiku i genetičko inženjerstvo, Beograd

Abstract

Penicillin G acylase (PAC) is one of the most widely used enzymes in industrial 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 (? and ?) of the enzyme were N-glycosylated, while the ?-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.

Publisher

National Library of Serbia

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology

Reference14 articles.

1. “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A

2. An Approach for Enhancing Heterologous Production of Providencia rettgeri Penicillin Acylase in Escherichia coli

3. Expression inPichia pastorisand Purification ofAspergillus awamoriGlucoamylase Catalytic Domain

4. Overexpression, Purification, and Characterization of Recombinant Barley α-Amylases 1 and 2 Secreted by the Methylotrophic YeastPichia pastoris

5. Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Potential of Pichia pastoris for the production of industrial penicillin G acylase;Folia Microbiologica;2017-03-09

2. Industrial and Therapeutic Enzymes;Current Developments in Biotechnology and Bioengineering;2017

3. Biotechnological advances on Penicillin G acylase: Pharmaceutical implications, unique expression mechanism and production strategies;Biotechnology Advances;2013-12

4. Gene cloning and soluble expression of Aspergillus niger phytase in E. coli cytosol via chaperone co-expression;Biotechnology Letters;2013-09-28