By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Enzymes and Coenzymes. According to news reporting originating in Jeonbuk, South Korea, by NewsRx journalists, research stated, "Metagenomic resources representing ruminal bacteria were screened for novel exocellulases using a robotic, high-throughput screening system, the novel CelEx-BR12 gene was identified and the predicted CelEx-BR12 protein was characterized. The CelEx-BR12 gene had an open reading frame (ORF) of 1140 base pairs that encoded a 380-amino-acid-protein with a predicted molecular mass of 41.8 kDa."
The news reporters obtained a quote from the research from the Korea Research Institute of Bioscience and Biotechnology, "The amino acid sequence was 83% identical to that of a family 5 glycosyl hydrolase from Prevotella ruminicola 23. Codon-optimized CelEx-BR12 was overexpressed in Escherichia coli and purified using Ni-NTA affinity chromatography. The Michaelis-Menten constant (K-m value) and maximal reaction velocity (V-max values) for exocellulase activity were 12.92 mu M and 1.55 x 10(-4) mu mol min(-1), respectively, and the enzyme was optimally active at pH 5.0 and 37 degrees C. Multifunctional activities were observed against fluorogenic and natural glycosides, such as 4-methylumbelliferyl-beta-D-cellobioside (0.3 U mg(-1)), CMC (105.9 U mg(-1)), birch wood xylan (132.3 U mg(-1)), oat spelt xylan (67.9 U mg(-1)), and 2-hydroxyethyl-cellulose (26.3 U mg(-1))."
According to the news reporters, the research concluded: "Based on these findings, we believe that CelEx-BR12 is an efficient multifunctional enzyme as endocellulase/exocellulase/xylanase activities that may prove useful for biotechnological applications."
For more information on this research see: A novel multifunctional cellulolytic enzyme screened from metagenomic resources representing ruminal bacteria. Biochemical and Biophysical Research Communications, 2013;441(3):567-572. Biochemical and Biophysical Research Communications can be contacted at: Academic Press Inc Elsevier Science, 525 B St, Ste 1900, San Diego, CA 92101-4495, USA. (Elsevier - www.elsevier.com; Biochemical and Biophysical Research Communications - www.elsevier.com/wps/product/cws_home/622790)
Our news correspondents report that additional information may be obtained by contacting K.C. Ko, Korea Res Inst Biosci & Biotechnol, Biorefinery Res Center, Jeongeup Si 580185, Jeonbuk, South Korea. Additional authors for this research include J.H. Lee, Y. Han, J.H. Choi and J.J. Song (see also Enzymes and Coenzymes).
Keywords for this news article include: Asia, Jeonbuk, South Korea, Enzymes and Coenzymes
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