Identification and characterization of emGalaseE, a β-1,4 galactosidase from Elizabethkingia meningoseptica, and its application on living cell surface

In this study, a unique beta 1,4 galactosidase was isolated from Elizabethkingia meningoseptica (Em). It exhibited favorable stability at various temperatures (4-37 °C) and pH (5-8) levels and can remove β-1, 4 linked galactoses directly from glycoproteins. Using Alanine scanning, we found that two acidic residues (Glu-468, and Glu-531) in the predicted active pocket are critical for galactosidase activity. In addition, we also demonstrated that it could cleave galactose residues present on living cell surface. As this enzyme has a potential application for living cell glycan editing, we named it emGalaseE or glycan-editing galactosidase I (csgeGalaseI). In summary, our findings lay the groundwork for further investigation by presenting a simple and effective approach for the removal of galactose moieties from cell surface.PMID:38657932 | DOI:10.1016/j.ijbiomac.2024.131766

Source: International Journal of Biological Macromolecules - April 24, 2024 Category: Biochemistry Authors: Yongliang Tong Xinrong Lu Danfeng Shen Lin Rao Lin Zou Shaoxian Lyu Linlin Hou Guiqin Sun Li Chen Source Type: research