Immobilization of beta-galactosidase for application in organic chemistry using a chelating peptide |
| |
Authors: | Piesecki S Teng W Y Hochuli E |
| |
Institution: | Hoffmann-La Roche, Inc., Nutley, New Jersey 07110. |
| |
Abstract: | The strong interaction of hexa-histidine fusion proteins with metal chelate adsorbents was utilized to immobilize beta-galactosidase with a hexa-histidine peptide at the N-terminus to the Ni(2+)-nitrilotriacetic acid adsorbent. The fusion protein was cloned and expressed in Escherichia coli. The purified soluble fusion protein showed the same specific activity as the purified beta-galactosidase and retained 64 percent of its beta-galactosidase activity when bound to the adsorbent. To demonstrate the potential of the immobilized beta-galactosidase in organic chemistry, allyl-beta-D-galactosidase was synthesized from lactose and allyl alcohol on a gram scale. The same enzyme preparation was reused in three subsequent batches to prepare the model compound with high yield. (c) 1993 John Wiley & Sons, Inc. |
| |
Keywords: | recombinant β-galactosidase fusion protein chelating peptide immobilized metal affinity chromatography immobilized enzyme |
本文献已被 PubMed 等数据库收录! |