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  • Title: Depiction of carbohydrate-active enzyme diversity in Caldicellulosiruptor sp. F32 at the genome level reveals insights into distinct polysaccharide degradation features.
    Author: Meng DD, Ying Y, Zhang KD, Lu M, Li FL.
    Journal: Mol Biosyst; 2015 Nov; 11(11):3164-73. PubMed ID: 26392378.
    Abstract:
    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 β-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 β-glucosidase BlgA synergistically facilitated the enzymatic degradation of Avicel by endo-1,4-β-glucanase CelB, which indicated that the synchronous action of synergism between CAZymes enhanced the lignocellulose degradation by Caldicellulosiruptor sp. F32.
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