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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Fig. 1

Chaetomella raphigera D2 strain secretes a β-glucosidase. C. raphigera was cultured for 4 days at 25 °C on PDA plates with (right) or without (left) β-glucoside esculin. Compared to the control plate (left), β-glucosidase activity is revealed by the presence of black precipitates in the PDA plate (right) supplied with 1 g/L esculin and 0.3 g/L ferric citrate as substrates

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