期刊论文详细信息
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】

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