ABSTRACT
This paper describes a particularly convenient technique for manipulating enzymes to be used in organic synthesis, in which soluble protein is enclosed in dialysis membranes. This type of containment facilitates separation of the enzyme from the reaction medium and allows its reuse. In many instances, enzyme stabilities equaled those observed with gel- or solid-immobilized enzymes. Enzymes remained active in the presence of water-miscible and water-immiscible organic solvents. Regeneration of both nicotinamide and nucleotide triphosphate cofactors was also possible using this technique. Modification of the membrane and how these changes relate to transport rates of different materials were also investigated. The use and limitations of using membrane-enclosed enzymes for practical organic synthesis is discussed.
