Nylon Digesting Bacteria
🧬 ★ Nylon-Digesting Bacteria:
Let’s first explain the story of nylon-digesting bacteria before we start responding to the evolutionists’ nonsense…
Researchers found a type of bacteria called Flavobacteria capable of digesting nylon 40 years after nylon was produced.
What’s so strange about that?!
The strange thing is that nylon wasn’t manufactured until 1935 , and it isn’t even a natural substance that bacteria can digest as is common.
They said, then, that these bacteria must have developed a new mechanism that enables them to digest nylon.
🪫 They concocted a story that would attract non-experts to present the myth on a golden platter.
They said that these bacteria had a frameshift mutation that led to the insertion of a nitrogenous base (T ) into the plasmid (pOAD2 ) within the R-llA sequence, leading to the emergence of the enzyme Nylonase , which enables bacteria to digest nylon…
📌 But before we respond, what are frameshift mutations ?
It is a type of mutation in which nitrogenous bases are added or deleted.
For example, the sequence of nitrogenous bases AGCTGGACT translates each three-letter codon into an amino acid linked to the translation of the next codon, and so on…
-
The codon AGC is translated into the amino acid Serine ,
-
followed by TGG which is translated into Tryptophan ,
-
followed by ACT which is translated into Threonine ,
meaning in this sequence we have Ser-Trp-Thr .
If an addition mutation occurs, for example, at the beginning of the sequence and the sequence becomes CAGCTGGACT , then different codons will be formed, and all of this is due to a displacement mutation…
Until now, you might think that this is blatant evidence of evolution, and that I have not responded to it;
but hold on… hold on…
This type of mutation has huge effects, and leads to protein distortion or the insertion of a premature stop codon that leads to the truncation and shortening of the protein;
but it does not even lead to the formation of a new enzyme…
❓ How?!
And isn’t the Nylonase enzyme evidence of the emergence of a completely new enzyme that was able to break down something that didn’t exist before?!!
🪫 Now we respond:
When you talk about laughter, give the example of the Arabs’ Darawneh.
They even cite studies from 2000 and 1984 , which were originally responded to in 2005 , yet they are determined to deceive;
🪫 Imagine how bankrupt they are, and then they say we are followers of science…
They don’t know that the enzyme that has a fold of the Beta Lactamase type has undergone slight modifications that made it able to include nylon in bacterial metabolic sequences.
https://pubmed.ncbi.nlm.nih.gov/16162506/
And for those who don’t know what protein folds are, in short: a protein only acquires a function when it undergoes a three-dimensional fold from specific sequences of amino acids. This is against them originally… in all cases against them… If a frameshift mutation actually occurred, this indicates its inability to change the enzyme’s fold, because displacement mutations lead to major changes, usually by inserting a premature stop codon that leads to cutting and shortening the protein, and these mutations lead to protein distortion;
https://www.sciencedirect.com/topics/neuroscience/frameshift-mutation
{Embed}
https://pubmed.ncbi.nlm.nih.gov/16162506/
X-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase…
6-Aminohexanoate-dimer hydrolase (EII), responsible for the degradation of nylon-6 industry by-products, and its analogous enzyme (EII’) that has only approximately 0.5% of the specific activity toward the 6-aminohexanoate-linear dimer, are encoded on plasmid pOAD2 of Arthrobacter sp. (formerly Flav …
But the reality is that Nylonase has the same protein folding as Beta Lactamase found in Carboxylesterase enzymes; That is, no stop or start codons were added, but rather a change in an existing fold. Incidentally, such changes are found in any organism. So, to say that a frameshift mutation led to the appearance of a new enzyme by chance cannot be more than a comedy or bedtime story. This enzyme is originally a promiscuity enzyme, which works in a wide range of decomposition of different materials. As long as the chemical bond that the enzyme works on is the same as that found in another material, it can break this bond, even if this material was invented recently. In short, what happened are improvements in the active site of the three-dimensional folding of Beta Lactamase found in the Carboxylesterase enzymes originally found in bacteria. So, there was no addition of a new fold, but rather modifications to the first fold. A new enzyme may result from a pre-existing fold. These improvements occur in any organism and are evidence of diversity within the genetic diversity stock of the same SGV species, as we explained in the article on mutations, and not modifications that led to… For additions that were not present.. and the same trick is promoted in many examples as an addition from outside the framework of the genetic diversity stock of the single species SGV, and studies later show that they are changes within the same species.. we propose that amino acid replacements in the catalytic cleft of a preexisting esterase with the beta-lactamase fold resulted in the evolution of the nylon oligomer hydrolase.
https://pubmed.ncbi.nlm.nih.gov/16162506/
{Embed}
https://pubmed.ncbi.nlm.nih.gov/16162506/
X-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase…
6-Aminohexanoate-dimer hydrolase (EII), responsible for the degradation of nylon-6 industry by-products, and its analogous enzyme (EII’) that has only approximately 0.5% of the specific activity toward the 6-aminohexanoate-linear dimer, are encoded on plasmid pOAD2 of Arthrobacter sp. (formerly Flav …
