Nylonase isn’t New Information
When discussing evolution on the internet, “nylonase” is often said to be the holy grail proof of evolutionary theory. Bacteria (specifically Flavobacterium, and Pseudomonas aeruginosa) have acquired the ability to digest a man-made product, nylon, which has only existed since 1935. It was originally proposed that a frameshift mutation acting on duplications caused the change. In other words, DNA was copied – creating more raw material to work with – and then changed by frameshift to give bacteria this digestion ability.
If this is really the case, then new information would have been added, because the original copy was kept and the duplication changed meaning. This would prove that evolutionary change has been observed and that evolutionary theory may be possible.
But the mechanism is under serious question. The four antisense DNA strands (1,535 base pairs) that underwent frameshift lack stop codons. Thus it is most unlikely that a frameshift mutation is the culprit for nylon digestion. Why is this? Frameshifts are known to produce a number of stop codons when they occur, and this would undoubtedly have happened in the supposed ‘evolution’ of nylonase enzymes. But they are lacking.
So how did nylon digestion come about? It seems it arose from a carboxyesterase gene which already had some capacity to degrade nylon oligomers. A team lead by Negoro proposed that the nylonase enzyme was derived from a pre-existing esterase enzyme.
But whichever way nylon digestion came about, evolutionists have yet to show it as an example of new information. Their frameshift/duplication explanation is seriously questionable. So the burden of proof is on the evolutionist if he wants to use it to bolster evolutionary theory.
- Ohno, S., “Birth of a unique enzyme from an alternative reading frame of the preexisted, internally repetitious coding sequence,” Proceedings of the National Academy of Sciences USA 81:2421–2425, 1984. Back to text
- Yomo, T., Urabe, I. and Okada, H., “No stop codons in the antisense strands of the genes for nylon oligomer degradation,” Proceedings of the National Academy of Sciences USA89:3780–3784, 1992. Back to text
- Negoro, S., et al., “Nylon-oligomer Degrading Enzyme/Substrate Complex: Catalytic Mechanism of 6-Aminohexanoate-dimer Hydrolase,” Journal of Molecular Biology, 370(1):142–156, 2007, ISSN 0022-2836, DOI: 10.1016/j.jmb.2007.04.043. Back to text