Technological Profile of Lipases in the Pharmaceutical Industry

Abstract

: In recent decades, enzymes have been the target of considerable research, development, and innovation. This paper presents an up-to-date overview of the technological application of lipases in the pharmaceutical industry. Lipases have been used in a variety of ways in the pharmaceutical industry, both in the obtainment of bioactive molecules to overcome limitations in the formulation of medicines and in drug design. This is possible from alternative technologies, such as immobilization and the use of non-aqueous solvents, which allows the use of lipases in commercial scale processes. In addition, other technologies have provided the emergence of differentiated and more specific lipases in order to meet the perspectives of industrial processes. The research indicates that the next years should be promising for the application of lipase in the industrial biocatalysis and in drug design.

Modulation of the Biocatalytic Properties of a Novel Lipase from Psychrophilic Serratia sp. (USBA-GBX-513) by Different Immobilization Strategies

“…A significant number of reversible and irreversible immobilization protocols have been developed to immobilize lipases [ 12 , 31 , 34 , 35 , 36 , 37 , 38 , 39 ]. Such immobilization strategies can improve enzyme stability and even the enantioselectivity or enantiospecificity of the biocatalyst if properly performed [ 16 ].…”

“…Immobilization methods included: interfacial adsorption on octyl agarose hydrophobic support (OC) [ 17 ], covalent binding on octyl glyoxyl Sepharose (OCGLX) after interfacial activation immobilization [ 44 , 45 , 46 ], direct covalent binding on CNBr-Sepharose [ 62 , 63 ], and anion exchange on Q-Sepharose [ 61 ]. The immobilized enzyme derivatives were compared with the commercial lipase B from Candida antarctica (CALB), immobilized on octyl Sepharose [ 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , ...…”

Various Strategies for the Immobilization of a Phospholipase C from Bacillus cereus for the Modulation of Its Biochemical Properties

“…Several reversible and irreversible immobilization approaches have been involved in enzyme immobilization [11][12][13][14]. One of the most commonly used techniques in the immobilization of lipases and some phospholipases is their immobilization on hydrophobic supports via interfacial activation.…”

Tuning Almond Lipase Features by Using Different Immobilization Supports

“…This is due to their robustness, lack of cofactors and wide specificity, and ability to accept a wide variety of substrates. Their high stability has enabled the use of lipases in a wide variety of reaction media (e.g., aqueous [7,8], organic solvents [2,9], supercritical fluids [10,11], ionic liquids [12][13][14][15][16], eutectic solvents [17,18], solvent-free systems [19]), and their variety of substrates permits to use them in a diversity of industrial areas [20] (wastewater treatment [21], food [22][23][24], energy [25,26], cosmetic [27], pharmaceutical [28][29][30], fine chemistry [31][32][33][34][35][36]). They can be used in hydrolysis [7,8], acidolysis [37,38], interesterifications [39,40], esterifications [19,41,42], transesterifications [25,43], amidations [44][45][46], etc.…”