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Abstract
Lipases are one of the most used enzymes in the pharmaceutical industry due to their efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an industrial viewpoint, the selection of an efficient expression system and host for recombinant lipase production is highly important. The most used hosts are Escherichia coli and Komagataella phaffii (previously known as Pichia pastoris) and less often reported Bacillus and Aspergillus strains. The use of efficient expression systems to overproduce homologous or heterologous lipases often require the use of strong promoters and the co-expression of chaperones. Protein engineering techniques, including rational design and directed evolution, are the most reported strategies for improving lipase characteristics. Additionally, lipases can be immobilized in different supports that enable improved properties and enzyme reuse. Here, we review approaches for strain and protein engineering, immobilization and the application of lipases in the pharmaceutical industry.
Highlights
Lipases have a myriad of industrial and biotechnological applications that rely on the variety of reactions that they catalyze
E. coli BL21 (DE3) strain was used as expression host and the best lipolytic activity was verified with the co-expression of the N-terminal truncated lipase gene with the full-length foldase gene
The results showed that, in Y. lipolytica, growth rate and detected CALB activity were higher than those achieved in K. phaffii
Summary
Lipases have a myriad of industrial and biotechnological applications that rely on the variety of reactions that they catalyze. Lipases have tremendous potential industrial use, they often need to have their properties improved due to the biocatalytic bioprocess requirements Using techniques, such as site directed mutagenesis based on rational design, different mutants can be constructed showing improved thermal stability, tolerance against organic solvents and optimized selectivity [36,37]. This is due to the necessity to achieve optimal performance in different industrial fields, and to effectively catalyze synthetic reactions in micro-aqueous conditions where organic solvents are required. There is major focus on the limitations and strategies used to overcome drawbacks found in lipase use reported in recent investigations
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