TY - JOUR
T1 - Advances in recombinant lipases: Production, engineering, immobilization and application in the pharmaceutical industry
AU - Jares Contesini, Fabiano
AU - Davanço, Marcelo Gomes
AU - Borin, Gustavo Pagotto
AU - Garcia Vanegas, Katherina
AU - Cirino, João Pedro Gonçalves
AU - de Melo, Ricardo Rodrigues
AU - Mortensen, Uffe Hasbro
AU - Hildén, Kristiina
AU - Campos, Daniel Rossi
AU - Carvalho, Patricia de Oliveira
PY - 2020
Y1 - 2020
N2 - 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.
AB - 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.
KW - Biocatalysis
KW - Industrial applications
KW - Sustainable chemistry
U2 - 10.3390/catal10091032
DO - 10.3390/catal10091032
M3 - Review
SN - 2073-4344
VL - 10
JO - Catalysts
JF - Catalysts
IS - 9
M1 - 1032
ER -