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Fig. 3 | BMC Biotechnology

Fig. 3

From: Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum

Fig. 3

Characterization of recombinant Xln-DT β-xylosidase. a Effects of optimum pH and pH stability of the enzyme Xln-DT; b Effect of temperature on Xln-DT activity; c The thermostability of the enzyme Xln-DT. The residual activity was monitored while the enzyme was incubated at 65 °C (filled diamonds), 75 °C (filled squares), 85 °C (flled triangles) and 95 °C (filled circles). The maximum activity was defined as 100%; d The kinetic of thermal inactivation of the enzyme Xln-DT at different temperatures ranging from 75 °C to 95 °C for several time intervals (75 °C (filled squares), 85 °C (filled circles), 95 °C (filled triangles))

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BMC Biotechnology

ISSN: 1472-6750

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