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- W2805771336 abstract "PBNXI is a recombinant plasmid containing vector plasmid pUC19 and a 2.6 kbfragment of Bacillus coagulans ST-6 genomic DNA which contains a xylanase gene.PBNX2 is another recombinant plasmid with the same insert DNA but in a pUC 18vector. Both plasmids expressed xylanase activity when grown on RBB-Xylan agarplates. Preliminary to nucleotide sequencing, the recombinant plasmids were modifiedusing restriction enzyme deletion to remove a segment of the insert DNA. The originalinsert DNA which was 2.6 kb was successfully reduced to a 0.8 kb and a 1.8 kbfragment in pBNXIA and pBNX2A respectively. The deletion was done usingrestriction endonuclease Sail and the resulting deletion mutants together with theoriginal clones were used to determine the nucleotide sequence of the xylanase gene.By primer walking, 1420 bp of the forward sequence was obtained where anopen reading frame (ORF) was found at 544 bp of the insert DNA. This 630 bp frame was preceeded by the putative E.coli - 10 and -35 promoters. No sequencecorresponding to the signal peptide was found in this sequence.The open reading frame (ORF) was translated into a peptide of 2 1 0 amino acidresidues. This protein belonged to Family G 11 of the Glycosyl Hydrolase family andhad 59% homology with Bacillus stearothermophilus xylanase and 54% homology withxylanase from Aeromonas caviae. Eleven out of 20 completely conserved amino acidsin this family were also conserved in this sequence and two conserved glutamateresidues, E 104 and E 186 were directly involved in the enzyme's acid-catalyticmechanism. Secondary structure prediction showed that this enzyme consisted of twoa-helices and 10 B-strands. Phylogenic studies showed that the primary structure of theenzyme was most closely related to Bacillus pumilus xylanase's primary structure.The analysis of the deduced amino acid sequence showed that there were fivecysteine residues in this sequence compared to none in four other mesophilic xylanases.These cysteine residues can form internal disulfide bonds among themselves which canincrease the stability of the protein. Analyzing the predicted secondary structure, anextra a-helical structure which is a more stable secondary structure was observed incomparison to other mesophilic xylanases. These two factors namely the presence ofcysteine residues and the extra a-helical structure may have an important role indetermining the thermo stability of this enzyme." @default.
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- W2805771336 date "1999-07-01" @default.
- W2805771336 modified "2023-09-27" @default.
- W2805771336 title "Determination of the Nucleotide Sequence of a Thermostable Xylanase Gene from Bacillus Coagulans ST-6" @default.
- W2805771336 hasPublicationYear "1999" @default.
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