화학공학소재연구정보센터
Process Biochemistry, Vol.43, No.7, 707-712, 2008
Purification and characterization of alpha-L-arabinofuranosidase from Arthrobacter sp MTCC 5214 in solid-state fermentation
Arthrobacter sp. MTCC 5214 produced an alpha-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 similar to 97 kDa. With p-nitrophenyl-alpha-L-arabinofuranoside as the substrate, the enzyme exhibited a K(m) of 0.3 mM, and a V(max) of 3.34 mu mol min(-1) mg(-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(2+) and Fe(2+) induced, whereas Hg(2+) inhibited the activity of the enzyme. To the best of our knowledge, this is the first report on the production of alpha-L-arabinofuranosidase by a bacterium when grown on solid-state fermentation. (C) 2008 Elsevier Ltd. All rights reserved.