Recovery and purification of aprotinin form industrial insulin- processing effluent by immobilized chymotrypsin and negative IMAC chromatographies

摘要

Aprotinin, a bovine protease inhibitor currently also produced in recombinant bacteria, yeast, and corn, ha valuable applications as a human therapeutic and in tissue culture. The objective of this work was to develop the basis of a large-scale aprotinin purification process centered on immobilized metal ion affinity chromatography (IMAC). This technique uses ligands-metal ions-of a lower cost and higher stability than those traditionally used in affinity chromatography. Since aprotinin does not interact with IMAC ligands, collection is from the nonretained fractions (negative chromatography).