To be honest, when I first read this article it was a bunch of mumbo jumbo in my mind. I was thinking: what the poop is it talking about??? I also doubt the title is relevant to the article but who cares. But, after reading it a few more time, it made more sense...light bulb moment!
Anyways, the abstract talks about how scientists were using the gene encoding endoxylanase (xynA) from Thermoanaerobacterium saccharolyticum B6A-RI. They cloned and expressed this gene in E. coli. Then xynA encoded a hypothetical 33-amino-acid signal peptide, which corresponded to the N-terminal amino acids. From doing this, there were findings of an open reading frame of 3,471 bp, which corresponds to 1,157 amino acid residues. These results gave xynA gene product a molecular mass of 130 kDa (Dalton).
According to the study, xynA from T. saccharolyticum B6A-RI had strong similarity to genes from family F beta-glycanases. The activity of the cloned endoxylanase had a temperature of 70 degrees C and a pH optimum of 5.5. The cloned endoxylanase A was stable at 75 degrees C for 60 min and displayed a specific activity of 227.4 U/mg of protein on oat spelt xylan (a substrate for the specific assay of endo-1,4-ß-D-xylanase). Therefore, scientists concluded that the cloned xylanase was an endo-acting enzyme, meaning that it contained functions within the cell in which it was produced...ain't that spiffy?
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