Lipase immobilization entrapment/encapsulation

Adsorption, hnkage, bonding of the enzyme to an insoluble support and entrapment of the enzyme in polymeric gels or encapsulation have all been used as ways to immobilise lipases [38]. To be successful, various parameters of the immobilization support need to be considered such as its mechanical strength, chemical and physical stability, its hydrophilicity/lipophilicity and the relevant loading capacity of the enzyme [39]. 

Microencapsulation is a similar technique to entrapment but less common. In this method, a membrane-Uke support is formed around the enzyme. Therefore, both the lipase and its environment are immobilized. Encapsulation can be carried out... 

The drawbacks of previous methods can be overcome by a combining two of any immobilization methods (Kanwar et al., 2004 Yadav and Jadhav, 2005 Zarcula et al., 2009). Ursoiu et al. (2011) deposited immobilized C. antarctica lipase B via sol-gel entrapment on support material. Yadav and Jadhav (2005) tested the preimmobilization of C. antarctica lipase B on hexagonal mesoporous silica using physical adsorption, followed by encapsulation in calcium alginate beads, which resulted in a reusable lipase with no leaching even after the fourth reuse. 

Traditional techniques such as physical adsorption and covalent linkage onto solid supports, entrapment in polymer matrices, and microencapsulation have long been used for immobilizing such enzymes as lipases, proteases, hydantoinases, acylases, amidases, oxidases, isomerases, lyases, and transferases [12-18]. Encapsulation and adsorption have also proved their utility in the immobilization of bacterial, fungal, animal, and plant cells [12-21]. However, as biocatalysis applications have grown, so the drawbacks and limitations of traditional approaches have become increasingly evident. The forefront issues now facing bioimmobilization are indicated in Table 1. 

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