Selective xyloglucan oligosaccharide hydrolysis by a GH31 α-xylosidase from Escherichia coli
In: Carbohydrate Polymers, Jg. 284 (2022-05-01), S. 119150-119150
Online
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Zugriff:
Xyloglucan is ubiquitous in the cell walls of land plants and is also an essential storage polymer in seeds of many species. We studied the hydrolysis of the non-reducing end xylosyl residue of xyloglucan oligosaccharides (XGOs) by the Escherichia coli α-xylosidase (YicI). Electrospray Ionization Tandem Mass Spectrometry (ESI-MS/MS) and ion fragmentation analysis together with high performance anion exchange chromatography with pulsed amperometric detection revealed that YicI preferentially removes the xylosyl residue from the glycosyl residue of non-galactosylated oligosaccharides. The YicI shows decreasing activity against the galactosylated oligosaccharides XXXGXXLG≥XLXG. Studies of the XGOs interaction with active site residues by molecular dynamics simulations suggested that hydrogen bond interactions between the D49 and galactosylated oligosaccharides play an important role in enzyme-XGO interactions. This was confirmed by site-directed mutagenesis, where the D49A mutant affected catalytic efficiency against galactosylated XGOs. Our findings advance xyloglucan disassembly models and highlight the importance of YicI for biotechnology applications.
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Selective xyloglucan oligosaccharide hydrolysis by a GH31 α-xylosidase from Escherichia coli
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Autor/in / Beteiligte Person: | Lara Aparecida Buffoni de Campos, Carneiro ; Carlos Alessandro, Fuzo ; Luana Parras, Meleiro ; Sibeli, Carli ; Matheus Quintana, Barreto ; Marcos Roberto, Lourenzoni ; Marcos Silveira, Buckeridge ; Richard John, Ward |
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Zeitschrift: | Carbohydrate Polymers, Jg. 284 (2022-05-01), S. 119150-119150 |
Veröffentlichung: | Elsevier BV, 2022 |
Medientyp: | unknown |
ISSN: | 0144-8617 (print) |
DOI: | 10.1016/j.carbpol.2022.119150 |
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