Purification and Some Properties of Intracellular α-L-Arabinofuranosidase from Aspergillus niger 5-16

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α-L-Arabinofuranosidase was purified from a cell-free extract of Aspergillus niger 5-16 by chromatographies on DEAE-Toyopearl, SP-Toyopearl, Ultro-gel AcA 44, Mono P, and TSK-GelG3000SW. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight and isoelectric point were 67,000 by SDS-polyacrylamide gel electrophoresis and pH 3.5by isoelectric focusing. The α-L-arabinofuranosidase contained amino acids in the order of Asx>Gly>Ala>Thr>Glx=Ser. The enzyme had maximum activity at pH 4.0 and 60℃, and was stable from pH 4 to 7 and at temperatures up to 30℃. The enzyme activity was not affected considerably by either metal ions or chemical reagents. The enzyme released arabinose from p-nitrophenyl-α-L-arabinofuranoside, O-α-L-arabinofuranosyl-(1→3)-O-β-D-xylopyranosyl-(1→4)-D-xylopyranose, and arabinan, but not from O-β-D-xylopyranosyl-(1→4)-O-[α-L-arabinofuranosyl-(1→3)]-O-β-D-xylopyranosyl-(1→4)-D-xylopyranose, O-β-D-xylopyranosyl-(1→2)-O-α-L-arabinofuranosyl-(1→3)-O-β-D-xylopyranosyl-(1→4)-O-β-D-xylopyranosyl-(1→4)-D-xylopyranose, gum arabic, or arabinoxylan. The limit of hydrolysis of arabinan was about 58% even when the enzyme was sufficiently in excess.
社団法人日本農芸化学会の論文
1993-07-23