1966 年 59 巻 6 号 p. 531-536
Enzyme activity for hydrolysis of cyclic and linear oligomers of 6-aminocaproic acid was found in cell extracts of Corynebacterium aacrantiacum B-2(S) and B-2(R), which are strains of bacteria selected by their ability to utilize e-caprolactam.
1. The preparations hydrolyzed cyclic and linear oligomers other than 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 6-amino-caproic acid.
2. When strain B-2(R) was cultured on cyclic trimer or tetramer, the cell extract showed a high activity to hydrolyze linear dimer as well as cyclic oligomers. The activity was lower when cells were cultured on ammonium adipate.
3. It seems probable that the cell extract of B-2(R) contains two enzyme systems, one which opens the ring of cyclic oligomers and the other which splits the chain of linear oligomers.
The author wishes to express his thanks to Prof. J. Ashida, Kyoto University, for his kind advice and criticism, and to Dr. K. Kato, Toyo Rayon Co., Ltd., for his valuable suggestions and encouragement in this work.