α-l-Arabinofuranosidase fromSclerotinia sclerotiorum: Purification, Characterization, and Effects on Plant Cell Walls and Tissue

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Abstract
S. sclerotiorum produced .alpha.-L-arabinofuranosidase when grown at 25.degree. C on a medium of mineral salts containing 0.4% L-arabinose plus 0.2% Difco yeast extract. Enzyme in filtrates from 14 day old cultures was concentrated and dialyzed by Amicon ultrafiltration. The specific activity of the .alpha.-L-arabinofuranosidase was increased 26 times by a 4-step procedure: preparative electrofocusing in granulated gel using ampholytes with a pH of 7-9; column ion-exchange chromatography (CM-Sephadex [C-50]) in 20 mM sodium acetate at pH 5.0; and 2 cycles of gel filtraton on Ultrogel (AcA 54) in 72 mM phosphate buffer at pH 7.0 containing 100 mM NaCl. Purified .alpha.-L-arabinofuranosidase had a pH optimum of 4.0-4.5, a MW of about 63,000 and a pI [isoelectric point] of about 7.5. This enzyme released arabinose from arabinan and from isolated cell walls of bean and rice. Highly active preparations of this .alpha.-L-arabinofuranosidase failed to macerate potato tuber or cucumber endocarp tissue.

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