ArticleBioprocess and biosystems engineering2026
Designing strategies for high-level production of peptide-N-glycosidase F (PNGase F) from Flavobacterium meningosepticum using high cell density fed-batch culture of E. coli.
Article in Bioprocess and biosystems engineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Protein N-glycosylation is a crucial post-translational modification that regulates cellular processes such as cell signalling, development, and autophagy. Abnormalities in protein glycosylation can manifest in life-threatening conditions, such as cancer. N-glycan analysis is crucial for determining the underlying cause of disease. The characterization of N-linked glycans is achieved through the removal of the carbohydrate moiety using deglycosylating enzymes. Peptide-N-glycosidase F (PNGase F) is a glycoamidase that hydrolyzes the amide bond in glycosamide by specifically cleaving at the innermost N-acetylglucosamine (GlcNAc). Although PNGase F has significant therapeutic applications, its widespread commercial use is limited by its high cost. This study focused on heterologous expression of Flavobacterium meningosepticum PNGase F in E. coli BL21 (DE3) and SHuffle
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