Advances in recombinant lipases: production, engineering, immobilization and application in the pharmaceutical industry

F. J. Contesini, M. G. Davanco, G. P. Boriin, K. G. Vanegas, J. P. G. Cirino, R. R. de Melo, U. H. Mortensen, K. Hilden, D. R. Campos, P. D. Carvalho

Research output: Contribution to journalArticlepeer-review

35 Downloads (Pure)


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.
Original languageEnglish
Article number1032
Number of pages33
Issue number9
Publication statusPublished - 9 Sept 2020


  • biocatalysis
  • industrial applications
  • sustainable chemistry

Cite this