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

M Gustavsson, J Lehtio, S Denman, TT Teeri, K Hult, M Martinelle*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)711-715
Number of pages5
JournalPROTEIN ENGINEERING
Volume14
Issue number9
Publication statusPublished - Sep 2001
MoE publication typeA1 Journal article-refereed

Keywords

  • Candida antarctica
  • cellulose-binding domain
  • lipase
  • proteolysis
  • STREPTOMYCES-LIVIDANS GLYCOSYLATES
  • CRYSTALLINE CELLULOSE
  • FIMI

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