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Discovery of Microorganisms and Enzymes Involved in High-Solids Decomposition of Rice Straw Using Metagenomic Analyses

机译:利用元基因组分析发现稻草高固体分解的微生物和酶

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摘要

High-solids incubations were performed to enrich for microbial communities and enzymes that decompose rice straw under mesophilic (35°C) and thermophilic (55°C) conditions. Thermophilic enrichments yielded a community that was 7.5 times more metabolically active on rice straw than mesophilic enrichments. Extracted xylanase and endoglucanse activities were also 2.6 and 13.4 times greater, respectively, for thermophilic enrichments. Metagenome sequencing was performed on enriched communities to determine community composition and mine for genes encoding lignocellulolytic enzymes. Proteobacteria were found to dominate the mesophilic community while Actinobacteria were most abundant in the thermophilic community. Analysis of protein family representation in each metagenome indicated that cellobiohydrolases containing carbohydrate binding module 2 (CBM2) were significantly overrepresented in the thermophilic community. Micromonospora, a member of Actinobacteria, primarily housed these genes in the thermophilic community. In light of these findings, Micromonospora and other closely related Actinobacteria genera appear to be promising sources of thermophilic lignocellulolytic enzymes for rice straw deconstruction under high-solids conditions. Furthermore, these discoveries warrant future research to determine if exoglucanases with CBM2 represent thermostable enzymes tolerant to the process conditions expected to be encountered during industrial biofuel production.
机译:进行高固体温育,以丰富在中温(35°C)和嗜热(55°C)条件下分解稻草的微生物群落和酶。嗜热性富集产生的群落在稻草上的代谢活性比嗜温性富集高7.5倍。对于嗜热性富集,提取的木聚糖酶和内切葡聚糖酶的活性也分别高2.6倍和13.4倍。对富集的社区进行了元基因组测序,以确定社区组成并挖掘编码木质纤维素分解酶的基因。发现变形杆菌在嗜温菌群落中占主导地位,而放线菌在嗜热菌群落中最为丰富。对每个元基因组中蛋白质家族表示的分析表明,在嗜热性社区中,含有碳水化合物结合模块2(CBM2)的纤维二糖水解酶明显超标。放线菌的一员微单孢菌主要将这些基因安置在嗜热菌群落中。根据这些发现,Micromonospora和其他紧密相关的放线菌属似乎是在高固含量条件下用于稻草解构的嗜热木质纤维素分解酶的有前途的来源。此外,这些发现需要进行进一步的研究,以确定具有CBM2的葡聚糖酶是否代表对工业生物燃料生产过程中可能遇到的工艺条件具有耐受性的热稳定酶。

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