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

Paper ID Volume ID Publish Year Pages File Format Full-Text
35567 45096 2008 6 PDF Available
Title
Purification and characterization of α-l-arabinofuranosidase from Arthrobacter sp. MTCC 5214 in solid-state fermentation
Abstract

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.

Keywords
Arthrobacter sp.; α-l-Arabinofuranosidase; Enzyme; Thermostability; Purification; SSF
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Purification and characterization of α-l-arabinofuranosidase from Arthrobacter sp. MTCC 5214 in solid-state fermentation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 7, July 2008, Pages 707–712
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
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