# The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method
## 7 Application of Lipases Immobilized on a Porous Support  
Many studies have been conducted on the immobilization of lipases on hydrophobic porous supports [56; 60; 63; 76]. Higher temperatures will break bond interactions within a protein structure that is responsible for a proper globular catalytic active structure [90; 91; 92; 93]. However, thermal effects become less prominent toward the immobilized lipase [90; 91]. Since a porous support has a large surface area for lipase adsorption, hierarchical porous polymers (HPSs) are used to immobilize phospholipase D and catalyze transphosphatidyl [37]. The optimum temperature for immobilizing phospholipase D is increased by 5 \({}^{\circ}\)C compared to that for free lipase. After 28 days, the immobilized phospholipase D still had 80% of activity, which is higher than free lipase [37]. The hydrolysis of triglyceride esters (high oleate sunflower oil) is catalyzed by _Candida rugosa_ lipase on a macroporous polyolefin support [64]. The immobilized _Candida rugosa_ lipase reaches half-life at a longer time compared to free lipase [24; 25]. Some advantages of immobilized lipase applications include reduced energy costs, shortened process times, prevention of loss of volatile compounds, and reduced risk of contamination [94; 95]. Besides, the reusability of lipases also increases after immobilization. A study showed the immobilized lipase B from _Candida rugosa_ was reused for six cycles of reaction to catalyze the esterification of free fatty acids obtained from soybean-oil hydrolysis and different polyols [96]. The same lipase from _Candida rugosa_ was immobilized and showed better storage stability than free lipase after four weeks of incubation [64]. The immobilized lipase from _Staphylococcus warneri_ (EX17) and _Burkholderia ambifaria_ (YCJ01) is used to catalyze the synthesis of short-chain esters, which has a fruity flavor similar to the pineapple, which can be used in flavors, fragrances, fine chemicals, and food industry [97; 98]. Soybean oil is used as substrates for the synthesis of fatty acid methyl esters by CALB and the glycerolysis of soybean oil by lecitase ultra (phospholipase) [99]. Immobilized lipase is vital for large-scale industrial production. The leading enzyme producers, such as Amano, Novozymes, DSM, and AB ENZYMES, have to supply various enzymes for industrial purposes [100]. Currently, practical systems that have already been adopted in industrial production are the industry sectors, such as fats and oleo-chemistry, detergent, polymers, biodiesel, and food processing [101]. These industry sectors utilize immobilized lipase to achieve the optimum condition for the large-scale industry production. For instance, the fats and oleo chemistry industry uses immobilized lipase to catalyze the hydrolysis, esterification, and inter-esterification of oils and fats as an alternative to physicochemical processes (energy-saving and the specificity of reactions) [100; 101]. The applications of immobilized lipase on porous supports under optimum conditions are listed in Table 3.  
\begin{table}
\begin{tabular}{c c c c c c c} \hline
**Source** & **Temperature (°C)** & **pH** & **Reusability** & **Stability** & **Application** & **Reference** \\ \hline Heterologous & & & & & Synthesis of human milk fat & [8] \\ _Ritzopus orange_ & 60 & 7 & 2 batches & - & & substitutes \\ _Cmida_ sp. (1.3170) & 25 & 7 & - & & In immobilized lipase: 2.4 h & Hydolysis of p-nitrophenyl & [31] \\ _Ritzopus orange_ & 37 & wide & 12 & 4 months & & n-butyl oleate synthesis by & [32] \\ _Ritzopus orange_ & 37 & wide & 12 & 4 months & & esterification of oleic acid with & [32] \\  & & & & & & n-butanol & \\  & &  
\begin{table}
\begin{tabular}{c c c c c c c} \hline
**Source** & **Temperature (CO)** & **pH** & **Reusability** & **Stability** & **Application** & **Reference** \\ \hline _Maver juveniles_ & & & Free lipase: 5; & & & & \\  & & & Inmobilized & - & & & \\  & & Free lipase: 7 & & lipase 30 & & & \\  & & & CALA/MB: 5 & & & & \\  &