title: Immobilization of beta-galactosidase for application in organic chemistry using a chelating peptide.
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.
authors.affiliation: Hoffmann-La Roche, Inc., Nutley, New Jersey 07110, USA.
authors.forename: S
authors.initials: S
authors.lastname: Piesecki
authors.forename: W Y
authors.initials: WY
authors.lastname: Teng
authors.forename: E
authors.initials: E
authors.lastname: Hochuli