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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Functional characterization of the native swollenin from Trichoderma reesei: study of its possible role as C1 factor of enzymatic lignocellulose conversion

Fig. 1

Identification, purification and deglycosylation of SWO1. a SWO1 (indicated with a rectangle) was recombinantly expressed in T. reesei QM9414 ∆xyr1 (designated as RJ_SWO1) and secreted into the culture media (two independent fermentations are shown). A prominent band at about 75 kDa, which was absent in an untransformed control strain, was identified as SWO1. b Single-step batch chromatography on Avicel PH-101 as adsorbent was used to purify SWO1 (two independent purifications are shown). The purified protein migrated as a single but relatively diffuse protein band, suggesting that the recombinant SWO1 was strongly glycosylated. c Deglycosylation of SWO1 with Endo H resulted in a decrease of the apparent molecular mass by roughly 5 kDa and a more sharply focused protein band was obtained in the SDS-polyacrylamide gel. d Direct glycostaining of the same gel shown in c confirmed the presence of glycans on both the native and the Endo H-treated SWO1

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