GLYCOSYLATION AND PH STABILITY OF PENICILLIN G ACYLASE FROM PROVIDENCIA RETTGERI PRODUCED IN PICHIA PASTORIS

被引：3

作者：

Senerovic, Lidija ^{[1
,2
]}

Stankovic, Nada ^{[1
]}

Ljubijankic, G. ^{[1
]}

Vasiljevic, Branka ^{[1
]}

机构：

[1] Inst Mol Genet & Genet Engn, Belgrade 11010, Serbia

[2] Max Planck Inst Infect Biol, D-10117 Berlin, Germany

来源：

ARCHIVES OF BIOLOGICAL SCIENCES | 2009年 / 61卷 / 04期

关键词：

Penicillin acylase; glycosylation; pH stability; Pichia pastoris; ESCHERICHIA-COLI; METHYLOTROPHIC YEAST; SACCHAROMYCES-CEREVISIAE; PURIFICATION; EXPRESSION; SECRETION; PROTEINS;

D O I：

10.2298/ABS0904581S

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

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 (alpha 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.

引用

页码：581 / 586

页数：6

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