Research Data from French National Institute for Agricultural Research (INRA) Update Understanding of Enzymes and Coenzymes [Four GH11 xylanases from the xylanolytic fungus Talaromyces versatilis act differently on (arabino)xylans]
By a News Reporter-Staff News Editor at Biotech Week -- Investigators publish new report on Enzymes and Coenzymes. According to news reporting originating in Nantes, France, by NewsRx journalists, research stated, "The filamentous fungus Talaromyces versatilis produces a wide range of cellulolytic and hemicellulolytic enzymes such as xylanases. The recent accessibility to the T. versatilis genome allows identifying two new genes, xynE and xynF, encoding glycoside-hydrolases from family GH11."
The news reporters obtained a quote from the research from French National Institute for Agricultural Research (INRA), "Both genes were cloned and expressed in the methylotrophic yeast Pichia pastoris in order to compare these new xylanases with two other GH11 xylanases from T. versatilis (XynB and XynC) that were previously reported. High-level expression of recombinant enzymes was obtained for the four enzymes that were purified to homogeneity. The XynB, XynC, XynE and XynF enzymes have molecular masses of 34, 22, 45 and 23 kDa, an optimal pH between 3.5 and 4.5 and an optimal temperature between 50 degrees C and 60 degrees C. Interestingly, XynF has shown the best thermal stability at 50 degrees C for at least 180 min with a weak loss of activity. The four xylanases catalysed hydrolysis of low viscosity arabinoxylan (LVAX) with K-m(app) between 11.5 and 23.0 mg.mL(-1) and k(cat)/K-m(app) 170 and 3,963 s(-1) mg(-1). mL. Further investigations on the rate and pattern of hydrolysis of the four enzymes on LVAX showed the predominant production of xylose, xylobiose and some (arabino) xylo-oligosaccharides as end products. The initial rate data from the hydrolysis of short xylo-oligosaccharides indicated that the catalytic efficiency increased with increasing degree of polymerisation of oligomer up to 6, suggesting that the specificity region of XynE and XynF spans at least six xylose residues."
According to the news reporters, the research concluded: "Because of their attractive properties, T. versatilis xylanases might be considered for biotechnological applications."
For more information on this research see: Four GH11 xylanases from the xylanolytic fungus Talaromyces versatilis act differently on (arabino)xylans. Applied Microbiology and Biotechnology, 2014;98(14):6339-6352. Applied Microbiology and Biotechnology can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Applied Microbiology and Biotechnology - www.springerlink.com/content/0175-7598/)
Our news correspondents report that additional information may be obtained by contacting M. Lafond, INRA, UR Biopolymeres Interact Assemblages 1268, F-44316 Nantes 03, France. Additional authors for this research include O. Guais, M. Maestracci, E. Bonnin and T. Giardina (see also Enzymes and Coenzymes).
Keywords for this news article include: Nantes, France, Europe, Enzymes and Coenzymes
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