ABSTRACT
This chapter focuses on lipase immobilization and its advantages over soluble lipases and its effect on physiochemical characteristics, namely, their activity and stability. The uses of soluble lipases in industry are quite limited due to their natural instability under certain operating conditions, such as at high temperature and shear stress. The immobilization of any enzyme can be carried out using different methods. These are classified into: adsorption on hydrophobic and ionic exchange resins, covalent attachment on highly activated supports, entrapment, and encapsulation in matrices. Immobilization of lipase onto a membrane offers many advantages, such as a low drop in pressure when continuously operated, and high operational stability with low external and internal diffusional resistance. The covalent attachment of enzymes on supports is another popular immobilization technique where enzymes are retained on the support surface by forming strong covalent bonds. The stability of lipase is one of its prominent properties that needs to be considered for improvement via immobilization.
