A plasmid encoding enzymes for nylon oligomer degradation: nucleotide sequence and analysis of pOAD2

Article Abstract:

The amino acid sequence of the Flavobacterium sp. K1723T1 plasmid pOAD2, which forms nylon degrading enzymes, is given. The plasmid consists of 45519 bp and contains 876 termination codons in the clockwise direction and 778 termination codons in the anticlockwise direction. The G+C content of the plasmid is high. The structure of the plasmid is similar to substances such as oligopeptide permeases and isopenicillin N-acyltransferase. The position of the genes forming the degradation enzymes on the genome map is given.

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Emergence of nylon oligomer degradation enzymes in Pseudomonas aeruginosa PAO through experimental evolution

Article Abstract:

When Pseudomonas aeruginosa PAO is grown in a culture containing 6-aminohexanoate (Ahx) which is a by-product of nylon-6, it acquires the ability to obtain carbon and nitrogen from the Ahx cyclic dimer (Acd). This ability of the bacteria to use Ahx is due to a genetic change and two new enzymes are produced which can hydrolyse the cyclic dimer of Ahx. This metabolic adaptation of Pseudomonas aeruginosa PAO is useful in the biodegradation of nylon-6.

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6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2

Article Abstract:

The isolation of alkalophilic, nylon oligomer-degrading bacteria, their genetic cloning and the characterization of their nylon oligomer-degrading enzymes are described. The 6-aminohexanoate oligomer hydrolases (NylC) from the alkalophilic strains are similar to the enzyme in neutrophilic Arthrobacter sp. but has superior thermostability and affinity for nylon-related substrates.

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