Abstract
Two kinds of enzymes which hydrolyze oligomers of 6-aminocaproic acid were isolated and partially purified from the cell extract of Corynebacterium aurantiacum B-2(R) by the fractionation with ammonium sulfate followed by diethylaminoethyl (DEAE)-cellulose column chro-matography. One of the enzymes cleaves cyclic oligomers and splits linear oligomers into linear dimer unit. The other enzyme splits linear oligomers into the 6-aminocaproic acid unit. The optimum pH of the former is 7.6 for cyclic tetramer and 8.1 for linear tetramer, and of the latter enzyme 8.6. Both enzymes did not require co-factor.

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