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• W2022986429 abstract "Whereas protein disulfide isomerase (PDI) and prolyl isomerase (PPI) are considered as efficient protein folding catalysts, very few large scale processes use them because of economical and technical limitations. PDI and PPI were successfully immobilized on cross-linked agarose beads. PDI inactivation during coupling reaction was overcome by oxidizing active site thiols with dimethylsulfoxide and led to a 64% active enzyme. Alternatively, PPI and PDI biotinylation resulted in 100% and 55–66% active enzymes respectively. The use of these modified catalysts suppresses post-refolding purification and enables the design of biochemical reactors. Several other possible applications are also discussed. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 645–649, 1997." @default.
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• W2022986429 date "1997-12-20" @default.
• W2022986429 modified "2023-10-16" @default.
• W2022986429 title "New formulae for folding catalysts make them multi-purpose enzymes" @default.
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• W2022986429 doi "https://doi.org/10.1002/(sici)1097-0290(19971220)56:6<645::aid-bit7>3.0.co;2-n" @default.
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