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Stability towards alkaline conditions can be engineered into a protein ligand
KTH, Superseded Departments, Biotechnology.ORCID iD: 0000-0003-4214-6991
KTH, Superseded Departments, Biotechnology.ORCID iD: 0000-0001-8993-048X
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2000 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 80, no 2, 169-178 p.Article in journal (Refereed) Published
Abstract [en]

One of the problems with a proteinaceous affinity ligand is their sensitivity to alkaline conditions. Here, we show that a simple and straightforward strategy consisting of replacing all asparagine residues with other amino acids can dramatically improve the chemical stability of a protein towards alkaline conditions. As a model, a Streptococcal albumin-binding domain (ABD) was used. The engineered variant showed higher stability towards 0.5 M NaOH, as well as higher thermal stability compared to its native counterpart. This protein engineering approach could potentially also be used for other protein ligands to eliminate the sensitivity to alkaline cleaning-in-place (CIP) conditions.

Place, publisher, year, edition, pages
2000. Vol. 80, no 2, 169-178 p.
Keyword [en]
albumin-binding domain, cleaning-in-place, deamidation, human serum albumin, protein engineering, serum albumin, deamidation, residues, asparaginyl, peptides
Identifiers
URN: urn:nbn:se:kth:diva-19869ISI: 000087955500009OAI: oai:DiVA.org:kth-19869DiVA: diva2:338561
Note
QC 20100525Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2017-12-12Bibliographically approved

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Nygren, Per-ÅkeUhlén, MathiasHober, Sophia

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