Hydrolysis of Cyclic and Linear Oligomers of 6-Aminocaproic Acid by a Bacterial Cell Extract*

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Abstract
Enzyme activity for hydrolysis of cyclic and linear oligomers of 6-aminocaproic acid was found in cell extracts of Corynebacterium aurantiacum B-2(S) and B-2(R), which are strains selected because of their ability to utilize [epsilon]-caprolactam. The preparations hydrolyzed cyclic and linear oligomers other than the cyclic dimer. The linear analogue and smaller linear oligomers were produced from a cyclic oligomer, and a series of smaller linear oligomers was produced from a linear oligomer. The final product was 8-aminocaproic acid. When strain B-2(R) was cultured on cyclic trimer or tetramer, the cell extract actively hydrolyzed linear dimer and cyclic oligomers. The activity was lower when cells were cultured on ammonium adipate. The cell extract of B-2(R) may contain 2 enzyme systems, one which opens the ring of cyclic oligomers and the other which splits the chain of linear oligomers.

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