Abstract
By dint of electric field given during the polymerization process, alkaline phosphatase from porcine intestine was immobilized asymmetrically in photocrosslinkable resin prepolymer membrane through entrapment. Catalytic activities of two sides of the membrane and the transport-catalysis behavior were measured.
It was found that the conversion of the substrate, present in one chamber, to the product and the transport of the latter to the other side of the membrane were more efficiently carried out when the enzyme distribution in the matrix was inclined to the side of the membrane facing to the substrate-free chamber.
The same procedure was successfully applied to coimmobilize alcohol dehydrogenase from equine liver and formaldehyde dehydrogenase from yeast in one membrane with different (complementary) distributions of the enzymes with respect to the membrane thickness.
