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Applied and Environmental Microbiology, April 2006, p. 2483-2490, Vol. 72, No. 4
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.4.2483-2490.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Paenibacillus curdlanolyticus Strain B-6 Xylanolytic-Cellulolytic Enzyme System That Degrades Insoluble Polysaccharides

Patthra Pason, Khin Lay Kyu,^* and Khanok Ratanakhanokchai

School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand

Received 3 April 2005/ Accepted 21 January 2006

A facultatively anaerobic bacterium, Paenibacillus curdlanolyticus B-6, isolated from an anaerobic digester produces an extracellular xylanolytic-cellulolytic enzyme system containing xylanase, ß-xylosidase, arabinofuranosidase, acetyl esterase, mannanase, carboxymethyl cellulase (CMCase), avicelase, cellobiohydrolase, ß-glucosidase, amylase, and chitinase when grown on xylan under aerobic conditions. During growth on xylan, the bacterial cells were found to adhere to xylan from the early exponential growth phase to the late stationary growth phase. Scanning electron microscopic analysis revealed the adhesion of cells to xylan. The crude enzyme preparation was found to be capable of binding to insoluble xylan and Avicel. The xylanolytic-cellulolytic enzyme system efficiently hydrolyzed insoluble xylan, Avicel, and corn hulls to soluble sugars that were exclusively xylose and glucose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of a crude enzyme preparation exhibited at least 17 proteins, and zymograms revealed multiple xylanases and cellulases containing 12 xylanases and 9 CMCases. The cellulose-binding proteins, which are mainly in a multienzyme complex, were isolated from the crude enzyme preparation by affinity purification on cellulose. This showed nine proteins by SDS-PAGE and eight xylanases and six CMCases on zymograms. Sephacryl S-300 gel filtration showed that the cellulose-binding proteins consisted of two multienzyme complexes with molecular masses of 1,450 and 400 kDa. The results indicated that the xylanolytic-cellulolytic enzyme system of this bacterium exists as multienzyme complexes.

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* Corresponding author. Mailing address: School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok 10140, Thailand. Phone: 662 470 7753. Fax: 662 452 3479. E-mail: khin.kyu{at}kmutt.ac.th.

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Applied and Environmental Microbiology, April 2006, p. 2483-2490, Vol. 72, No. 4
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.4.2483-2490.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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