| Archives of Biological Sciences | |
| Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris | |
| 关键词: Penicillin acylase; glycosylation; pH stability; Pichia pastoris; | |
| DOI : 10.2298/ABS0904581S | |
| 来源: DOAJ | |
【 摘 要 】
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 (α and β) of the enzyme were N-glycosylated, while the β-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.
【 授权许可】
Unknown