The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris

• Published in: Microbial cell factories Vol. 21; no. 1; pp. 1 - 13
• Main Authors: Wang, Nan, Yang, Caifeng, Peng, Huakang, Guo, Wenfang, Wang, Mengqi, Li, Gangqiang, Liu, Dehu
• Format: Journal Article
• Language: English
• Published: London BioMed Central Ltd 30.08.2022; BioMed Central; BMC
• Subjects: Amino acids; Analysis; Annotations; Bacterial proteins; Chemical properties; Chymosin; Differential interacting proteins; Endoplasmic reticulum; Enzymatic activity; Enzymes; Glucose; Glucosyltransferase; Glycoproteins; Glycosylation; Immunoprecipitation; Industrial applications; Influence; Intracellular; Manufacturing industry; Mass spectrometry; Mass spectroscopy; Metabolism; Microorganisms; Molecular weight; Mutation; N-glycosylation; Pichia pastoris; Post-translation; Prochymosin; Protein folding; Protein-protein interactions; Proteins; Scientific imaging; Secretion; Signal transduction; Thermal stability; Yeast; China

N-glycosylation is one of the most important post-translational modifications. Many studies have shown that N-glycosylation has a significant effect on the secretion level of heterologous glycoproteins in yeast cells. However, there have been few studies reporting a clear and unified explanation for...