Immobilized chymotrypsin by means of Schiff base copper(II) chelate.
A new method for cross-linking of protein was proposed in our previous work. The method is based on the spontaneous chelate formation process involving three components, salicylaldehyde moiety, alpha-amino acid residue and copper(II). In this paper versatility of the method as a purpose of immobilization of enzyme was described. Chymotrypsin-salicylaldehyde conjugate was immobilized to the agarose gel attached alpha-amino acid residue in the presence of copper(II) ion The enzyme was not eluted from the gel by washing with a copper free buffer though it was exclusively eluted by a medium containing EDTA. Catalytic activity of the chymotrypsin salicylaldehyde conjugate was not changed upon the immobilization. The method was proposed as a new tool for reversible immobilization of enzyme.
Moriya
K
K
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Tanizawa
K
K
Kanaoka
Y
Y
D000447:Aldehydes; D000818:Animals; D002384:Catalysis; D002417:Cattle; D002614:Chelating Agents; D002918:Chymotrypsin; D002919:Chymotrypsinogen; D003300:Copper; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D006868:Hydrolysis; D007700:Kinetics; D012545:Schiff Bases
D000447:Aldehydes; D002614:Chelating Agents; D004800:Enzymes, Immobilized; D012545:Schiff Bases; C013243:salicylaldehyde; D003300:Copper; D002919:Chymotrypsinogen; D002918:Chymotrypsin