Stable linker peptides for a cellulose-binding domain-lipase fusion protein expressed in Pichia pastoris

被引：80

作者：

Gustavsson, M ^{[1
]}

Lehtiö, J ^{[1
]}

Denman, S ^{[1
]}

Teeri, TT ^{[1
]}

Hult, K ^{[1
]}

Martinelle, M ^{[1
]}

机构：

[1] Stockholm Ctr Phys Astron & Biotechnol, Royal Inst Technol, Dept Biotechnol, S-10691 Stockholm, Sweden

来源：

PROTEIN ENGINEERING | 2001年 / 14卷 / 09期

关键词：

Candida antarctica; cellulose-binding domain; lipase; proteolysis;

D O I：

10.1093/protein/14.9.711

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fusion proteins composed of a cellulose-binding domain from Neocallimastix patriciarum cellulase A and Candida antarctica lipase B were constructed using different linker peptides. The aim was to create proteolytically stable linkers that were able to join the functional modules without disrupting their function. Six fusion variants containing linkers of 4-44 residues were expressed in Pichia pastoris and analysed. Three variants were found to be stable throughout 7-day cultivations. The cellulose-binding capacities of fusion proteins containing short linkers were slightly lower compared with those containing long linkers. The lipase-specific activities of all variants, in solution or immobilized on to cellulose, were equal to that of the wildtype lipase.

引用

页码：711 / 715

页数：5

共 19 条

[1] AN INVESTIGATION OF OLIGOPEPTIDES LINKING DOMAINS IN PROTEIN TERTIARY STRUCTURES AND POSSIBLE CANDIDATES FOR GENERAL GENE FUSION [J].