Immobilized lipases as practical catalysts

Abstract

Attractive features of lipase systems include versatility, substrate selectivity, regioselectivity, enantioselectivity and catalysis at ambient temperatures and pressures. To fully exploit the technical and economical advantages of lipases, it is recommended to use them in an immobilized form to reduce the cost and the poor stability of the free lipase. This paper summarizes various methods of lipases immobilization including covalent attachment to or adsorption on solid supports, encapsulation and entrapment within the membrane and in polymeric matrices. The effects of immobilization conditions on lipase properties and stability of biocatalysts are considered. Applications of immobilized lipases in the feasible reaction system as well as probable future trends in lipase catalyzed process are discussed.