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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency

Fig. 1

Overview of BxlB glycomutants. BxlBwt N-glycosylation sites were predicted by the NetNGlyc server, and all of these sites were validated by LC–MS/MS (orange circles). Three glycomutants were synthesized: BxlBN1;5;7, N-to-Q mutation of four validated N-glycosylated sites; BxlBnon-glyc, N-to-Q mutation of the seven predicted N-glycosylation sites; BxlBCC, addition of four new sites using BxlBnon-glyc as a template, to change the N-glycosylation context (purple circles), N121 (A123T), Q166 N, Q391 N, and N448 (L450T). Six additional mutants were designed by using the BxlBnon-glyc as a template maintaining individual N-glycosylation sites (BxlBN1, BxlBN5, BxlBN7) or combining two sites (BxlBN1;5, BxlBN5;7, BxlBN1;7). SP: signal peptide, N: amino-terminus, C: carboxy-terminus

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