Reversible denaturation of carbonic anhydrase provides a method for its adsorptive immobilization
Palmityl‐substituted sepharose 4B has been used for adsorptive immobilization of heat‐denatured carbonic anhydrase. The native form of this enzyme does not show any affinity for binding to this hydrophobic support. However, through the process of denaturation–renaturation performed by heating and su...
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Veröffentlicht in: | Biotechnology and bioengineering 1999-01, Vol.62 (2), p.193-199 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Palmityl‐substituted sepharose 4B has been used for adsorptive immobilization of heat‐denatured carbonic anhydrase. The native form of this enzyme does not show any affinity for binding to this hydrophobic support. However, through the process of denaturation–renaturation performed by heating and subsequent cooling of an enzyme solution in the presence of the matrix, it was possible to obtain a catalytically active immobilized preparation, which was used successfully in continuous catalytic transformations.
It is suggested that this simple procedure may provide a convenient method of immobilization for proteins, which are not normally adsorbed on hydrophobic supports. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 62: 193–199, 1999. |
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ISSN: | 0006-3592 1097-0290 |
DOI: | 10.1002/(SICI)1097-0290(19990120)62:2<193::AID-BIT9>3.0.CO;2-H |