期刊文献+

热纤梭菌高效降解木质纤维素过程的组学研究进展 被引量:6

Mics of the Clostridium thermocellum in lignocellulose degradation—A review
原文传递
导出
摘要 热纤梭菌(Clostridium thermocellum)是高效降解木质纤维素的重要微生物,因其能分泌纤维小体这一超分子酶系复合物而备受关注。它分泌的酶系组分多样,胞外酶组分的表达、分泌及其在纤维小体支架蛋白上的组装是一受到胞外碳源等因素显著影响的动态过程。热纤梭菌究竟如何感知纤维素等不溶性底物的存在并动态调控相应酶组分的分泌,完成具有高效降解能力的超分子酶系复合物的组装成为近几年来相关研究的热点。本文主要从基因组学、转录组学、蛋白质组学及菌体对胞外碳源的感应机制等方面来综述相关研究进展,并对热纤梭菌降解天然复杂生物质的动态过程及其相应机制进行了剖析,并展望其应用前景。 Clostridium thermoceUum (C. thermocellum ) is the dominant microorganism that can efficiently degrade lignocellulose. Extensive studies were done for secreting the cell surface-bound protein complex known as the cellulosome. C. thermocellum is regulated by carbon sources, reflected in overall multiple cellulase production and in the cellulosomal subunit profile. To produce a cellulosomal protein complex is a dynamic assembly process. In recent years, it becomes a hotspot to study how C. thermocellum senses the insoluble substrate, regulates the secretion of relevant enzymes, and assembles the supramolecular-degradation enzyme complex. This review summarized the research advance in genomics, transcriptomics, proteomies and extracellular carbohydrate-sensing mechanism in C. thermoceUum, and analyzed the mechanism and dynamic process of C. thermocellum in lignocellulose degradation.
机构地区 山东大学
出处 《微生物学报》 CAS CSCD 北大核心 2014年第2期121-128,共8页 Acta Microbiologica Sinica
基金 国家“973项目”(2011CB707401) 国家“863计划”(2012AA10180402) 山东省国际科技合作项目计划(鲁科合字[2011]176号第6项)~~
关键词 热纤梭菌 基因组学 转录组学 蛋白组学 感应机制 Clostridium thermocellum, genomics, transcriptomics, proteomics, carbohydrate-sensing mechanism
  • 相关文献

参考文献1

二级参考文献48

  • 1Ragauskas A J, Williams C K, Davison B H, et al. The path forward for biofuels and biomaterials. Science, 2006, 311(5760): 484-489.
  • 2Lynd L R, van Zyl W H, McBride J E, et al. Consolidated bioprocessing of cellulosic biomass: an update. Curt Opin Biotechnol, 2005, 16(5): 577-583.
  • 3Bayer E A, Belaich J P, Shoham Y, et al. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annu Rev Microbiol, 2004, 58:521-554.
  • 4Doi R H, Kosugi A. Cellulosomes: plant-cell-wall-degrading enzyme complexes. Nat Rev Microbiol, 2004, 2(7): 541-551.
  • 5Ding S Y, Rincon M T, Lamed R, et al. Cellulosomal scaffoldin- like proteins from Ruminococcus flavefaciens. J Bacteriol, 2001, 183(6): 1945-1953.
  • 6Rincon M T, Ding S Y, McCrae S I, et al. Novel organization and divergent dockerin specificities in the cellulosome system of Ruminoeoceus flavefaeiens. J Bacteriol, 2003, 185(3): 703-713.
  • 7Shimon L J, Bayer E A, Morag E, et al. A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure, 1997, 5(3): 381-390.
  • 8Noach I, Frolow F, Jakoby H, et al. Crystal structure of a type- Ⅱ cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements. J Mol Biol, 2005, 348(1): 1-12.
  • 9Lytle B L, Volkman B F, Westler W M, et al. Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium- binding domain. J Mol Biol, 2001, 307(3): 745 753.
  • 10Adams J J, Webb B A, Spencer H L, et al. Structural characterization of type Ⅱ dockerin module from the cellulosome of Clostridium therrtmcellum: calcium-induced effects on conformation and target recognition. Biochemistry, 2005, 44(6): 2173-2182.

共引文献9

同被引文献74

引证文献6

二级引证文献28

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部