An arabinase has been purified from the culture fluid of Erwinia carotovora IAM 1024 grown on a mediumcontaining arabinan. The purified enzymewas active on beet arabinan and inactive on 1, 5-arabinan, arabinoxylan, arabinogalactan, and p-nitrophenyl α-L-arabinofuranoside. The optimumpH was 6.0. The enzyme was stable over a pH range of5.0 to 1 1.0. Whenthe purified enzyme acted on beet arabinan, the main product was arabinotriose.

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