4.5 Article

An extremely thermophilic anaerobic bacterium Caldicellulosiruptor sp F32 exhibits distinctive properties in growth and xylanases during xylan hydrolysis

期刊

ENZYME AND MICROBIAL TECHNOLOGY
卷 53, 期 3, 页码 194-199

出版社

ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2013.04.004

关键词

Lignocellulosic biomass; Caldicellulosiruptor sp.; Xylanase; Hyperthermophile; Anaerobe

资金

  1. National Basic Research Program of China [2011CB707404]
  2. National Key Technology R&D Research Program [2011BAD22B02-01]

向作者/读者索取更多资源

An anaerobic, extremely thermophilic, and cellulose- and xylan-degrading bacterium F32 was isolated from biocompost. Sequence analysis of the 16S rRNA gene of this strain showed that it was closely related to Caldicellulosiruptor saccharolyticus DSM 8903 (99.0% identity). Physiological and biochemical data also supported that identification of strain F32 as a Caldicellulosiruptor species. The proteins secreted by Caldicellulosiruptor sp. F32 grown on xylan showed a xylanase activity of 7.74 U/mg, which was 2.5 times higher than that of C saccharolyticus DSM 8903. Based on the genomic sequencing data, 2 xylanase genes, JX030400 and JX030401, were identified in Caldicellulosiruptor sp. F32. The xylanase encoded by JX030401 shared 97% identity with Csac_0696 of C saccharolyticus DSM 8903, while that encoded by JX030400 shared 94% identity with Athe_0089 of C bescii DSM 6725, which was not found in the genome of strain DSM 8903. Xylanse encoded by JX030400 had 9-fold higher specific activity than JX030401. Our results indicated that although the 2 strains shared high identity, the xylanase system in Caldicellulosiruptor sp. F32 was more efficient than that in C. saccharolyticus DSM 8903. (C) 2013 Elsevier Inc. All rights reserved.

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