## 5 Application of Recombinant Lipases  
The versatility of lipases in catalyzing the hydrolysis of esters and reactions of esterification, trans-esterification and inter-esterification, considerably expands the commercial and technological applications of these enzymes. For this reason, they can be applied in the food, oleochemical, pharmaceutical, fine chemical, cosmetics, pulp and paper, leather and biosensor industries and in the treatment of effluents rich in oils and fats [155; 156; 157]. In addition, they have been used for the synthesis of different oleochemical products, such as free fatty acids, glycerin and its derivatives, biodiesel, biolubricants and different alkyl esters [158].  
Despite the vast application potential of the lipases, their application spectrum is limited due to an absence of the process-suitable characteristics necessary to endure harsh processing conditions during industrial applications operating at relatively high temperature and pH conditions. Hence, the lipases envisioned for industrially applicable processes must possess the necessary characteristics, such as stability and high yield, in order to prove their worth. The use of lipases as industrial catalysts depends heavily on the production of recombinant enzymes with biochemical and catalytic characteristics improved by protein engineering. The evolution of strategies to apply these techniques on an industrial scale has enabled a significant reduction in lipase cost, consequently stimulating the development of other industrial applications.  
Lipases are commonly applied in the dairy industry for the selective hydrolysis of milk triacylglycerglycerols during cheese ripening. Particularly, a lipase from _R. miehei_ expressed in _A. oryzae_ is commercially available with the trade name Palatase M (Novozymes) and used in the dairy industry to improve cheese properties. Lipase (Est_p6) isolated from a metagenomic library from marine sediments was produced in _E. coli_ and applied to efficiently hydrolyze milk fat and impart a desirable and distinctive flavor to milk products [159]. A _Penicillium cyclopium_ lipase produced in _K. phaffii_[160] has been used for the synthesis of mono- and diacylglycerols and showed its potential for food emulsifier preparations. The commercial enzyme Novozym 435, an immobilized lipase from _C. antarctica_ expressed in _A. niger_, has been successfully used to produce sugar esters [161].  
Specifically, in the pharmaceutical industry, recombinant enzymes are mainly used for applications as biocatalysts in the synthesis of chiral intermediates for the development of drugs, and as therapeutic drugs for the treatment of various diseases. Lipases offer several advantages compared to other enzymes and several chemical catalysts, such as capacity for the resolution of racemic mixtures by the synthesis of a simple enantiomer being currently exploited for the production of medicines by the pharmaceutical industry, mainly for the manufacturing of antidepressant, antihypertensive and vasodilator drugs [156; 162].  
Single-enantiomer intermediate synthesis for the preparation of drugs is important in the pharmaceutical industry. Single enantiomers can be produced either by chemical or biocatalytic routes. Biocatalysis is emerging as an efficient alternative to traditional chemical methods for the production of pharmaceuticals. The advantages of the enzyme-catalyzed reactions compared to chemical processes include enantioselectivity and the use of mild reaction conditions which may reduce energy consumption and waste generation.  
The following reported examples show that recombinant lipases have been an important tool in improving pharmaceutical processes for chiral drug intermediates and vitamin synthesis.