Purification and characterization of α-l-arabinofuranosidase from Arthrobacter sp. MTCC 5214 in solid-state fermentation

Arthrobacter sp. MTCC 5214 produced an α-l-arabinofuranosidase when grown on solid-state fermentation (SSF). The enzyme was purified 19-fold using ion exchange and gel filtration chromatography. The enzyme had an apparent molecular mass of ∼97 kDa. With p-nitrophenyl-α-l-arabinofuranoside as the substrate, the enzyme exhibited a Km of 0.3 mM, and a Vmax of 3.34 μmol min−1 mg−1. The enzyme had optimum activity at pH 8 and 80 °C. At pH 8.0 the enzyme was stable at 50 and 60 °C for 24 h, whereas it retained 90% of its activity after incubation at 70 °C for 3 h. Metal ions such as Co2+ and Fe2+ induced, whereas Hg2+ inhibited the activity of the enzyme. To the best of our knowledge, this is the first report on the production of α-l-arabinofuranosidase by a bacterium when grown on solid-state fermentation.