Development of recombinant human granulocyte colony-stimulating factor (nartograstim) production process in Escherichia coli compatible with industrial scale and with no antibiotics in the culture medium

Eguia, Fara A. P.; Mascarelli, Daniele Enriquetto; Carvalho, Enéas; Rodríguez, Gretel Rodríguez; Makiyama, Edson Naoto; Borelli, Primavera; Lieberman, Celia; Ho, Paulo Lee; Barazzone, Giovana Cappio; Gonçalves, Viviane Maimoni

doi:10.1007/s00253-020-11014-y

Cited by 4 publications

(2 citation statements)

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“…In the biopharmaceutical industry, E. coli is regarded as the first‐choice microorganism for the production of recombinant nonglycosylated proteins. However, when using E. coli for the industrial production of therapeutic molecules, regulatory quality aspects should be considered 92,93,96–104 . Although some E. coli strains have the ability to produce a toxin, most of them are harmless and even useful mainly in recombinant protein production.…”

Section: Expression Hostsmentioning

confidence: 99%

“…However, when using E. coli for the industrial production of therapeutic molecules, regulatory quality aspects should be considered. 92,93,[96][97][98][99][100][101][102][103][104] Although some E. coli strains have the ability to produce a toxin, most of them are harmless and even useful mainly in recombinant protein production. Maksum et al produced β-galactosidase in a wildtype E. coli B130 strain.…”

Section: Hosts For the Expression Of Bacterial β-Galactosidases Genementioning

confidence: 99%

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β‐Galactosidase: From its source and applications to its recombinant form

Movahedpour

Ahmadi

Ghalamfarsa

et al. 2021

Biotech and App Biochem

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Carbohydrate-active enzymes are a group of important enzymes playing a critical role in the degradation and synthesis of carbohydrates. Glycosidases can hydrolyze glycosides into oligosaccharides, polysaccharides, and glycoconjugates via a cost-effective approach. Lactase is an important member of β-glycosidases found in higher plants, animals, and microorganisms. β-Galactosidases can be used to degrade the milk lactose for making lactose-free milk, which is sweeter than regular milk and is suitable for lactose-intolerant people. β-Galactosidase is employed by many food industries to degrade lactose and improve the digestibility, sweetness, solubility, and flavor of dairy products. β-Galactosidase enzymes have various families and are applied in the food-processing industries such as hydrolyzed-milk products, whey, and galactooligosaccharides. Thus, this enzyme is a valuable protein which is now produced by recombinant technology. In this review, origins, structure, recombinant production, and critical modifications of β-galactosidase for improving the production process are discussed. Since β-galactosidase is a valuable enzyme in industry and health care, a study of its various aspects is important in industrial biotechnology and applied biochemistry.

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Section: Expression Hostsmentioning

confidence: 99%