Isolation and Characterization of Endocellulase-Free Multienzyme Complex from Newly Isolated Thermoanaerobacterium hermosaccharolyticum Strain NOI-1
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Author list: Chimtong S., Tachaapaikoon C., Pason P., Kyu K.L., Kosugi A., Mori Y., Ratanakhanokcha K.
Publisher: The Korean Society for Applied Microbiology
Publication year: 2011
Journal: Journal of Microbiology and Biotechnology (1017-7825)
Volume number: 21
Issue number: 3
Start page: 284
End page: 292
Number of pages: 9
ISSN: 1017-7825
Languages: English-Great Britain (EN-GB)
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Abstract
An endocellulase-free multienzyme complex was produced by a thermophilic anaerobic bacterium, Thermoanaerobacterium thermosaccharolyticum strain NOI-1, when grown on xylan. The temperature and pH optima for growth were 60°C and 6.0, respectively. The bacterial cells were found to adhere to insoluble xylan and Avicel. A scanning electron microscopy analysis showed the adhesion of xylan to the cells. An endocellulase-free multienzyme complex was isolated from the crude enzyme of strain NOI-1 by affinity purification on cellulose and Sephacryl S-300 gel filtration. The molecular mass of the multienzyme complex was estimated to be about 1,200 kDa. The multienzyme complex showed one protein on native PAGE, one xylanase on a native zymogram, 21 proteins on SDS-PAGE, and 5 xylanases on a SDS zymogram. The multienzyme complex consisted of xylanase, β-xylosidase, α-L-arabinofuranosidase, β-glucosidase, and cellobiohydrolase. The multienzyme complex was effective in hydrolyzing xylan and corn hulls. This is the first report of an endocellulase-free multienzyme complex produced by a thermophilic anaerobic bacterium, T. thermosaccharolyticum strain NOI-1. © The Korean Soceity for Microbiology and Biotechnology.
Keywords
Endo cellulase-free multienzyme complex, Thermoanaerobacterium thermosaccharolyticum, Thermophilic anaerobic bacterium
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