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Stable linker peptides for a cellulose-binding domain-lipase fusion protein expressed in Pichia pastoris
KTH, Superseded Departments, Biotechnology.
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2001 (English)In: Protein Engineering, ISSN 0269-2139, E-ISSN 1460-213X, Vol. 14, no 9, 711-715 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2001. Vol. 14, no 9, 711-715 p.
Keyword [en]
Candida antarctica, cellulose-binding domain, lipase, proteolysis, streptomyces-lividans glycosylates, crystalline cellulose, fimi
URN: urn:nbn:se:kth:diva-21127ISI: 000172378900014OAI: diva2:339824
QC 20100525Available from: 2010-08-10 Created: 2010-08-10Bibliographically approved

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