Stability towards alkaline conditions can be engineered into a protein ligand
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
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.
albumin-binding domain, cleaning-in-place, deamidation, human serum albumin, protein engineering, serum albumin, deamidation, residues, asparaginyl, peptides
IdentifiersURN: urn:nbn:se:kth:diva-19869ISI: 000087955500009OAI: oai:DiVA.org:kth-19869DiVA: diva2:338561
QC 201005252010-08-102010-08-10Bibliographically approved