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Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

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 impo...

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Bibliographic Details
Published in:Catalysts 2020-09, Vol.10 (9), p.1032
Main Authors: Contesini, Fabiano Jares, Davanço, Marcelo Gomes, Borin, Gustavo Pagotto, Vanegas, Katherina Garcia, Cirino, João Pedro Gonçalves, Melo, Ricardo Rodrigues de, Mortensen, Uffe Hasbro, Hildén, Kristiina, Campos, Daniel Rossi, Carvalho, Patricia de Oliveira
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Language:English
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Summary: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.
ISSN:2073-4344
2073-4344
DOI:10.3390/catal10091032