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Isolation and Some Properties of New Xylanase from the Intestine of a Herbivorous Insect (Samia Cynthia Pryeri)
Xylan the major portion of the hemicellulose of plant cell walls are heterogeneous polysaccharides. Xylanases are enzymes obtained from different species of microorganisms that degrade the xylosidic linkages of xylans backbone producing xylose with other monoresidues. In this study, xylanase producing strains were isolated from intestine of a herbivorous insect at Rajshahi University Campus. The strains were isolated on xylan agar media and screened by -xylanolysis method. Zymogram analysis was confirmed the xylanolytic activity. The strains was identified to be Aeromonas sp. and xylanase enzyme was detected in the culture supernatant of the strain. Xylanase enzyme was purified from culture supernatant of Aeromonas sp. by ammonium sulfate precipitation, gel filtration on Sephadex G-100 followed by ion exchange chromotography on DEAE-cellulose. In DEAE cellulose column chromatography, three protein peaks F-1a, F-1b and F-1c were appeared. Among these peaks, only F-1b showed xylanase activity and the degree of purification attained 64.54 fold. The purified enzyme gave single band on SDS-polyacrylamide gel electrophoresis indicating its homogeneity. The enzyme gave maximum activity against xylan as substrate at pH 7.0 and temperature at 55C. The Km value of xylanase was found to be 0.91% using the oat spelt xylan as substrate. The xylanase hydrolyzed strongly oat spelt xylan and birch wood xylan but didnot hydrolyze cellulose, carboxymethyl cellulose and starch. Xylose was detected as the hydrolysis products of oat spelt xylan by the xylanase.
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Correlation between nucleotide composition and folding energy of coding sequences with special attention to wobble bases
Background: The secondary structure and complexity of mRNA influences its accessibility to regulatory molecules (proteins, micro-RNAs), its stability and its level of expression. The mobile elements of the RNA sequence, the wobble bases, are expected to regulate the formation of structures encompassing coding sequences. Results: The sequence/folding energy (FE) relationship was studied by statistical, bioinformatic methods in 90 CDS containing 26,370 codons. I found that the FE (dG) associated with coding sequences is significant and negative (407 kcal/1000 bases, mean ± S.E.M.) indicating that these sequences are able to form structures. However, the FE has only a small free component, less than 10% of the total. The contribution of the 1st and 3rd codon bases to the FE is larger than the contribution of the 2nd (central) bases. It is possible to achieve a ~4-fold change in FE by altering the wobble bases in synonymous codons. The sequence/FE relationship can be described with a simple algorithm, and the total FE can be predicted solely from the sequence composition of the nucleic acid. The contributions of different synonymous codons to the FE are additive and one codon cannot replace another. The accumulated contributions of synonymous codons of an amino acid to the total folding energy of an mRNA is strongly correlated to the relative amount of that amino acid in the translated protein. Conclusion: Synonymous codons are not interchangable with regard to their role in determining the mRNA FE and the relative amounts of amino acids in the translated protein, even if they are indistinguishable in respect of amino acid coding.
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Akita University: Research Leaders and Postdoctoral Fellows
Research Leaders and Postdoctoral Fellows, Akita University, Akita, Japan. Posted on 25 July 2007.
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OHSU commercial collaborations have surged
(Oregon Health & Science University) Industry research collaborations -- or sponsored research agreements -- entered into by Oregon Health & Science University produced income in fiscal year 2008 of nearly $10 million, the OHSU Office of Technology & Research Collaborations reported today.
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[BOOK REVIEWS] Advances in Functional and Reparative Neurosurgery (Acta Neurochirurgica Supplementum), Supplement 99
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Microscope Stereoscopic
Welcome to WordPress. This is your first post. Edit or delete it, then start blogging!
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Weddings Site Reviews Latest Additions
By editor@weddingssitereviews.com - Copyright 2008 by the American Association for the Advancement of Science - version: v1.5 build A