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Please use this identifier to cite or link to this item: http://hdl.handle.net/2264/1092

Title: Purification and characterization of alpha-L-arabinofuranosidase from Arthrobacter sp. MTCC 5214 in solid-state fermentation
Authors: Khandeparker, R.
Numan, M.T.H.
Mukherjee, B.
Satwekar, A.
Bhosle, N.B.
Citation: Process Biochemistry, vol.43(7); 707-712p.
Issue Date: 2008
Publisher: Elsevier
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.
Document type: Journal Article
Copyright: Copyright Elsevier[2008]. It is tried to respect the rights of the copyright holders to the best of the knowledge. If it is brought to our notice that the rights are violated then the item would be withdrawn.
URI: http://hdl.handle.net/2264/1092
Appears in Collections:Biological Sciences

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