Fig. 1
Properties of PfCBH1. a The schematic representation of the amino acid sequence encoded by the PfCBH1 gene. The picture was generated with IBS v1.0 (http://ibs.biocuckoo.org/); signal peptides prediction was made using services of the SignalP 4.1 server (http://www.cbs.dtu.dk/services/SignalP/) and domain prediction with Pfam (http://pfam.xfam.org/). b The SDS-PAGE and Western blot confirmation using anti-PfCBH1 polyclonal antibody. Crude enzyme (lane 1) from the most performing secretome of P. funiculosum was subjected to hydrophobic interaction chromatography (lane 2), followed by anion exchange chromatography separation of active fractions (lane 3), the flow through was further subjected to hydrophobic interaction chromatography (lane 4) yielding pure CBH1 enzyme. M is a protein molecular weight marker. c The thermal stability of purified PfCBH1 under different pH conditions. The Tm optimal and pH are reported as amplitudes and means of the Gaussian fittings, respectively. d The relative Avicelase activity of purified PfCBH1 under different pH and temperature conditions. e The Lineweaver–Burk plot revealing the competitive nature of the inhibition by cellobiose. f The Log(inhibitor) vs. response curve for IC50 determination. Data are expressed as a percentage of uninhibited activity. A Hill slope of −1.6 was obtained implying a reduction in affinity for pNPL in the presence of cellobiose. g The hydrolysis of oligosaccharides by PfCBH1. The oligosaccharides tested are cellobiose (G2), cellotriose (G3), cellotetraose (G4), cellopentaose (G5), and cellohexaose (G6)