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Findings from Pennsylvania State University Provide New Insights into Biochemistry and Biotechnology (Purification and Characterization of Novel...

August 19, 2014



Findings from Pennsylvania State University Provide New Insights into Biochemistry and Biotechnology (Purification and Characterization of Novel Halo-Acid-Alkali-Thermo-stable Xylanase from Gracilibacillus sp TSCPVG)

By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Biochemistry and Biotechnology have been presented. According to news originating from University Park, Pennsylvania, by NewsRx correspondents, research stated, "An aerobic xylanolytic moderately halophilic and alkali-tolerant bacterium, Gracilibacillus sp. TSCPVG, produces multiple xylanases of unusual halo-acid-alkali-thermo-stable nature."

Our news journalists obtained a quote from the research from Pennsylvania State University, "The purification of a major xylanase from TSCPVG culture supernatant was achieved by hydrophobic and gel permeation chromatographic methods followed by electroelution from preparatory PAGE. The molecular mass of the purified xylanase was 42 kDa, as analyzed by SDS-PAGE, with a pI value of 6.1. It exhibited maximal activity in 3.5 % NaCl and retained over 75 % of its activity across the broad salinity range of 0-30 % NaCl, indicating a high halo-tolerance. It showed maximal activity at pH 7.5 and had retained 63 % of its activity at pH 5.0 and 73 % at pH 10.5, signifying the tolerance to broad acid to alkaline conditions. With birchwood xylan as a substrate, K (m) and specific activity values were 21 mg/ml and 1,667 U/mg, respectively. It is an endoxylanase that degrades xylan to xylose and xylobiose and had no activity on p-nitrophenyl-beta-d-xylopyranoside, p-nitrophenyl-beta-d-glucopyranoside, p-nitrophenyl acetate, carboxymethylcellulose, and filter paper."

According to the news editors, the research concluded: "Since it showed remarkable stability over different salinities, broad pH, and temperature ranges, it is promising for application in many industries."

For more information on this research see: Purification and Characterization of Novel Halo-Acid-Alkali-Thermo-stable Xylanase from Gracilibacillus sp TSCPVG. Applied Biochemistry and Biotechnology, 2014;173(6):1375-1390. Applied Biochemistry and Biotechnology can be contacted at: Humana Press Inc, 999 Riverview Drive Suite 208, Totowa, NJ 07512, USA. (Springer - www.springer.com; Applied Biochemistry and Biotechnology - www.springerlink.com/content/0273-2289/)

The news correspondents report that additional information may be obtained from V.G. Poosarla, Pennsylvania State University, University Park, PA 16802, United States (see also Biochemistry and Biotechnology).

Keywords for this news article include: Xylanase, Pennsylvania, United States, University Park, Enzymes and Coenzymes, North and Central America, Biochemistry and Biotechnology

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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