Partial characterization of β-glucosidase, β-xylosidase, and α-l-arabinofuranosidase from Jiangella alba DSM 45237 and their potential in lignocellulose-based biorefining

Jiangella alba DSM 45237 exhibited excellent extracellular β-glucosidase (1.03 ± 0.09 U/mL), β-xylosidase (16.29 ± 0.23 U/mL), and α-l-arabinofuranosidase (7.00 ± 0.09 U/mL) production in the growth media containing 15 g/L wheat straw pretreated with NaOH. The optimum temperature was 40 °C for β-glucosidase and β-xylosidase, whereas it was 50 °C for α-l-arabinofuranosidase. Among them, α-l-arabinofuranosidase was relatively stable at 60 and 70 °C. Enzymes showed maximum activity at pH 8.0. Enzymes, particularly β-glucosidase and α-l-arabinofuranosidase, were able to tolerate NaCl up to a final concentration of 12% (v/w). Among solvents, only ethanol and methanol increased the β-glucosidase activity. The majority of solvents did not significantly affect β-xylosidase activity but increased α-l-arabinofuranosidase activity. Except for phenol, other lignocellulose-derived compounds did not cause a significant activity loss in enzymes. Some of them, such as vanillic acid and acetic acid, have even increased the activity of enzymes. Hydrolysis of pretreated wheat straw using the crude enzyme from J. alba DSM 45237 released 160.9 mg/gds reducing sugars. Analysis of hydrolysis products with thin layer chromatography (TLC) showed that major products were 5C sugars. This is the first report related to the characterization of β-glucosidase, β-xylosidase, and α-l-arabinofuranosidase from J.alba DSM 45237 to date. [Display omitted] •Jiangella alba DSM 45237 is a potential producer of extracellular β-glucosidase, β-xylosidase and α-l-arabinofuranosidase.•Enzymes exhibit high activity in presence of NaCl, chemicals, solvents, and lignocellulose-derived compounds.•The crude enzyme can be used as a cellulase supplement to increase the hydrolysis efficiency of lignocellulosic biomass.