TY - JOUR
T1 - Advances in recombinant lipases
T2 - Production, engineering, immobilization and application in the pharmaceutical industry
AU - Contesini, Fabiano Jares
AU - Davanço, Marcelo Gomes
AU - Borin, Gustavo Pagotto
AU - Vanegas, Katherina Garcia
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
N1 - Funding Information:
We would like to thank FAPESP (Fundação de Amparo à Pesquisa do Estado de São Paulo), process numbers 2006/013932 and 2018/13317-6. We would like to acknowledge the EU/RIA Falcon project (720918) and Finnish Academy consortium project AromaFung (2988892) and the scholarship provided by FAPESP to R.R.d.M. (17/14253-9).
Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2020/9/9
Y1 - 2020/9/9
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
UR - http://www.scopus.com/inward/record.url?scp=85090638421&partnerID=8YFLogxK
U2 - 10.3390/catal10091032
DO - 10.3390/catal10091032
M3 - Article
AN - SCOPUS:85090638421
SN - 2073-4344
VL - 10
JO - Catalysts
JF - Catalysts
IS - 9
M1 - 1032
ER -
