Immobilization of alkaline phosphatase on cellulose magnetic particles activated by divinyl sulfone

Abstract

Investigation of properties of bovine intestinal alkaline phosphatase from intestinal mucosa immobilized to magnetic particles after activation with divinyl sulfone via the protein free amino groups. The effect of different conditions on the activity of soluble and immobilized forms of alkaline phosphatase was compared: the effect of pH, temperature and Mg(II) ions, storage stability and possibility of repeated use of the immobilized enzyme.

Keywords

• alkaline phosphatase
• magnetic particles
• properties of phosohatase