Skip to main content
Fig. 3 | Biotechnology for Biofuels

Fig. 3

From: A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity

Fig. 3

Characterization of the purified recombinant Ac-Abf51A with 4-nitrophenyl-α-L-arabinofuranoside as the substrate. a The effect of pH on enzyme activity. The activity assays were performed at 60 °C in buffers of pH 3.0–10.0 for 10 min. b pH stability of Ac-Abf51A. After pre-incubating the enzyme at 37 °C for 1 h at pH 3.0–12.0, the residual activities were measured in 100 mM McIlvaine buffer (pH 6.0, 60 °C and 10 min). c The effect of temperature on enzyme activity measured in 100 mM McIlvaine buffer (pH 6.0) for 10 min. d Thermostability of purified Ac-Abf51A. The enzyme was pre-incubated at 70 °C or 80 °C in 100 mM McIlvaine buffer (pH 6.0) for various periods, followed by activity assay at pH 6.0 and 60 °C for 10 min

Back to article page