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

Abstract

Arthrobacter sp. MTCC 5214 produced an a-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 approx. 97 kDa. With p-nitrophenyl-alpha-L-arabinofuranoside as the substrate, the enzyme exhibited a K sub(m) of 0.3 mM, and a V sub(max) of 3.34 mu mol min sup(-1) mg sup(-1). The enzyme had optimum activity at pH 8 and 80 degrees C. At pH 8.0 the enzyme was stable at 50 and 60 degrees C for 24 h, whereas it retained 90% of its activity after incubation at 70 degrees C for 3 h. Metal ions such as Co sup(2+) and Fe sup(2+) induced, whereas Hg sup(2+) inhibited the activity of the enzyme. To the best of our knowledge, this is the first report on the production of a-L-arabinofuranosidase by a bacterium when grown on solid-state fermentation.