Abstract
An endo-l,5-α-L-arabinase [EC 3.2.1.99] has been highly purified from the culture fluid of Bacillus subtilis IFO 3022 grown on a medium containing beet pulp extract. The molecular weight of the enzyme was 33,000 by SDS polyacrylamide gel electrophoresis. The purified enzyme was active on 1,5-arabinan, and inactive on p-nitrophenyl α-L-arabinofuranoside. The optimum pH was 6.0. The enzyme was inhibited by Hg2 + , but not by l-arabonic-γ-lactone. The purified enzyme was able to loosen potato tissue.