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Fig. 4 | Biotechnology for Biofuels

Fig. 4

From: Uncovering the molecular mechanisms of lignocellulose digestion in shipworms

Fig. 4

Characterization of LpMDGH1. a Schematic diagram of the architecture of the multi-domain GH1 from L. pedicellatus (LpMDGH1), featuring an N-terminal signal peptide for secretion and six distinct GH1 domains (numbered from 1 to 6) connected by short peptide linkers. b Maximum likelihood radial phylogeny of a subset of multi-domain GH1 proteins identified by BlastP search versus NCBI nr databases. c SDS-PAGE (denaturing and non-denaturing) and zymogram of soluble cecum fluids (s) and purified L. pedicellatus LpMDGH1 (p) using the chromogenic substrate 5-bromo-4-chloro-3-indolyl-β-d-cellobioside. A commercial protein marker (m) has been run in the same gel, with numbers representing the molecular weight of the protein bands in kDa. d Histogram showing the nanomoles of reducing sugars (as determined via DNS assay) released by the purified LpMDGH1 from cellobiose (c2), cellotriose (c3), cellotetraose (c4) cellopentaose (c5), cellohexaose (c6), xylobiose (×2), mannobiose (m2), konjac glucomannan (GM), barley β-glucan (βG), lichenan (L) and pachyman (P). Activity assays with insoluble polysaccharides included 1 mg mL−1 substrate. Activity assays with soluble oligosaccharides included 2.5 mM substrate. Bars indicate means (error bars: standard deviations of three replicates)

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