Hydrogel ultrafiltration of recombinant alkaline phosphatase from baculovirus-infected Spodoptera frugiperda

Abstract

Recombinant alkaline phosphatase expressed in insect cells was concentrated 1.5 times by hydrogel ultrafiltration by swelling at 20°C and collapsing at 35°C at 53-65% separation efficiency and 78-83% enzyme recovery. Enzyme entrapment between gel particles and attachment of enzymes to the gel surface was the main reason for the poor separation efficiency and low enzyme recovery. Exposure of the enzyme at the collapse temperature during repeated swelling-collapsing cycles also decreased separation efficiency to 37% due to thermal deactivation of the enzyme.