Depiction of carbohydrate-active enzyme diversity in Caldicellulosiruptor sp F32 at the genome level reveals insights into distinct polysaccharide degradation features
文献类型: 外文期刊
作者: Meng, Dong-Dong 1 ; Ying, Yu 1 ; Zhang, Kun-Di 1 ; Lu, Ming 1 ; Li, Fu-Li 1 ;
作者机构: 1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Key Lab Biofuels, Shandong Prov Key Lab Energy Genet, Qingdao 266101, Peoples R China
2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China
期刊名称:MOLECULAR BIOSYSTEMS ( 影响因子:3.336; 五年影响因子:2.986 )
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收录情况: SCI
摘要: Thermophilic bacterium Caldicellulosiruptor sp. F32 can utilize cellulose-, hemicellulose-containing biomass, including unpretreated wheat straw. We have conducted a bioinformatics analysis of the carbohydrate-active enzyme (CAZyme) in the genome of Caldicellulosiruptor sp. F32, which reveals a broad substrate range of the strain. Among 2285 predicted open reading frames (ORFs), 73 (3.2%) CAZyme encoding genes, including 44 glycoside hydrolases (GHs) distributing in 22 GH families, 6 carbohydrate esterases (CEs), 3 polysaccharide lyases (PLs), 21 glycosyl transferases (GTs), and 25 carbohydrate-binding modules (CBMs) were found. An in-depth bioinformatics analysis of CAZyme families that target cellulose, hemicellulose, chitin, pectin, starch, and beta-1,3-1,4-glucan degradation were performed to highlight specialized polysaccharide degrading abilities of strain F32. A great number of orthologous multimodular CAZymes of Caldicellulosiruptor sp. F32 were found in other strains of genus Caldicellulosiruptor. While, a portion of the CAZymes of Caldicellulosiruptor sp. F32 showed sequence identity with proteins from strains of genus Clostridium. A thermostable beta-glucosidase BlgA synergistically facilitated the enzymatic degradation of Avicel by endo-1,4-beta-glucanase CelB, which indicated that the synchronous action of synergism between CAZymes enhanced the lignocellulose degradation by Caldicellulosiruptor sp. F32.
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