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International Journal of Innovative Approaches in Science Research 2024, Vol 8(2) 70-78

Recombinat Production and Characterization of the SUMO-Tagged N-Glycosidase F Enzyme

Sercan Karav
Cite this article
Article Type
Research article
Publication Date
June 30, 2024
Pages
70-78
DOI
10.29329/ijiasr.2024.1054.3

Abstract

Glycans, a key component of cells, are abundant and diverse biopolymers found in covalent bonds of sucrose attached to proteins and lipids. They significantly contribute to mass and structural variation in biological systems. In order to characterize glycans, study their effects in various experiments, and comprehend their roles, it is necessary to isolate them from the proteins with which they are associated. Chemical methods and various enzymes separate glycans. The ease of application of chemical methods, despite their low cost, chemical methods ease of application affects the chemical structure of both glycans and the remaining part of the polypeptide during deglycosylation. Additionally, the high salt content of the separated glycans makes mass spectrometry analysis of these glycants difficult. For these reasons, the use of enzymes in glycan studies has increased in recent years. One of the most commonly used enzymes in this field, N-glycosidase F has a wide spectrum and the ability to successfully release various N-glycan structures from glycoprotein.

In this study, the PNGase F enzyme, secreted by Flavobacterium meningosepticum, was efficiently produced in a recombinant manner. The enzyme, which contains 314 amino acids, is the most effective method for removing N-glycan from glycoproteins.

Keywords: N-linked glycans Glycoproteins Glycosidases Deglycosylation In vivo cloning
Cite this article
Karav, S. (2024). Recombinat Production and Characterization of the SUMO-Tagged N-Glycosidase F Enzyme. International Journal of Innovative Approaches in Science Research, 8(2), 70-78. https://doi.org/10.29329/ijiasr.2024.1054.3

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