A novel multienzyme complex from a newly isolated facultative anaerobic bacterium, Paenibacillus sp. TW1
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Author list: Tachaapaikoon C., Kyu K., Pason P., Ratanakhanockchai K.
Publisher: Akadémiai Kiadó
Publication year: 2012
Journal: Acta Biologica Hungarica (0236-5383)
Volume number: 63
Issue number: 2
Start page: 288
End page: 300
Number of pages: 13
ISSN: 0236-5383
Languages: English-Great Britain (EN-GB)
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Abstract
A multienzyme complex from newly isolated Paenibacillus sp. TW1 was purified from pellet-bound enzyme preparations by elution with 0.25% sucrose and 1.0% triethylamine (TEA), ultrafiltration and Sephacryl S-400 gel filtration chromatography. The purified multienzyme complex showed a single protein band on non-denaturing polyacrylamide gel electrophoresis (native-PAGE). The high molecular mass of the purified multienzyme complex was approximately 1,950 kDa. The complex consisted of xylanase and cellulase activities as the major and minor enzyme subunits, respectively. The complex appeared as at least 18 protein bands on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and as 15 xylanases and 6 cellulases on zymograms. The purified multienzyme complex contained xylanase, α-L-arabinofuranosidase, carboxymethyl cellulase (CMCase), avicelase and cellobiohydrolase. The complex could effectively hydrolyze corn hulls, corncobs and sugarcane bagasse. These results indicate that the multienzyme complex that is produced by this bacterium is a large, novel xylanolytic-cellulolytic enzyme complex. © 2012 Akadémiai Kiadó, Budapest.
Keywords
Enzyme purification, facultative anaerobic bacterium, Multienzyme complex, Paenibacillus sp TW1, xylanolytic-cellulolytic enzymes
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