Two Extremely Thermostable Xylanases of the Hyperthermophilic Bacterium Thermotoga maritima MSB8.

Applied and Environmental Microbiology
C Winterhalter, W Liebl

Abstract

During growth with xylose or xylan as the source of carbon, xylanase production by Thermotoga maritima MSB8 was enhanced about 10-fold compared with growth with glucose or starch. Two extremely thermostable endoxylanases (1,4-(beta)-d-xylan-xylanohydrolase, EC 3.2.1.8), designated XynA and XynB, were identified and purified from cells of this organism. XynA and XynB occurred as proteins with apparent molecular masses of about 120 and 40 kDa, respectively, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Maximum activity at the optimal pH (pH 6.2 and pH 5.4 for XynA and XynB, respectively) was measured at about 92(deg)C for XynA (10-min assay) and at about 105(deg)C for XynB (5-min assay). XynB activity was stimulated twofold by the addition of 500 mM NaCl, while XynA displayed maximum activity without the addition of salt. Both xylanases were tolerant of relatively high salt concentrations. At 2 M (about 12% wt/vol) NaCl, XynA and XynB retained 49 and 65%, respectively, of their maximum activities. In contrast to XynB, XynA was able to adsorb to microcrystalline cellulose. Antibodies raised against a recombinant truncated XynA protein cross-reacted with XynB, indicating that the enzymes may have seque...Continue Reading

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Citations

Jul 31, 2014·Extremophiles : Life Under Extreme Conditions·Niwat ChawachartOssi Turunen
Jan 1, 1997·Critical Reviews in Biotechnology·A Sunna, G Antranikian
Mar 22, 2006·Extremophiles : Life Under Extreme Conditions·Jörg Kleine, Wolfgang Liebl
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Jan 28, 2014·Extremophiles : Life Under Extreme Conditions·Xiaoshuang LiuZiduo Liu
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