Purification and Characterization of an α-l-Arabinofuranosidase from Butyrivibrio fibrisolvens GS113

摘要: An alpha-l-arabinofuranosidase (EC 3.2.1.55) was purified from the cytoplasm of Butyrivibrio fibrisolvens GS113. The native enzyme had an apparent molecular mass 240 kDa and composed eight polypeptide subunits 31 kDa. displayed isoelectric point 6.0, a pH optimum 6.0 to 6.5, stability 4.0 8.0, temperature 45 degrees C stable 55 C. K(m) V(max) for p-nitrophenyl-alpha-l-arabinofuranoside were 0.7 mM 109 mumol/min/mg protein, respectively. specific furanoside configuration also readily cleaved methylumbelliferyl-alpha-l-arabinofuranoside but no activity on variety other nitrophenyl- or methylumbelliferyl glycosides. When incubated with cellulose, carboxymethyl arabinogalactan, release sugars found. Arabinose found as hydrolysis product oatspelt xylan, corn endosperm beet arabinan. No detected when either coumaric ferulic acid ester linked arabinoxylobiose used substrates, degraded arabinose xylobiose. Since B. GS113 possesses essentially extracellular arabinofuranosidase activity, major role is apparently in assimilation arabinose-containing xylooligosaccharides generated xylosidase, phenolic esterase, xylanase, enzymatic activities xylans.