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- W1993936731 abstract "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 in 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." @default.
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- W1993936731 date "2000-06-23" @default.
- W1993936731 modified "2023-10-15" @default.
- W1993936731 title "Stability towards alkaline conditions can be engineered into a protein ligand" @default.
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- W1993936731 doi "https://doi.org/10.1016/s0168-1656(00)00259-5" @default.
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