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Cloning and Expression of A Novel Gene Encoded Thermostable Archaeal Aldolase Class II from Natural Sample

机译:天然样品中编码新基因II类热稳定古生代醛缩酶的克隆与表达

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A novel class II Aldolase was isolated through metagenomic approach from Domas Crater, West Java, Indonesia. Sequence analysis of the enzyme was highly homolog to archaeal ribuIose-5-phosphate 4-epimerase from uncultured Acidilobussp. with percent identityof 63%. Homological analysis of the protein shows that the protein sequence contains all conserved motifs of aldolase class II. The enzyme shows Zn2+ binding, polypeptide binding, and active sites as other aldolase's. Phylogenetic analysis of the enzyme showed that the enzyme makes a different branch closed to ribulose-5-phosphate 4-epimerase of unculcured Acidilobus sp. The gene was expressed in E coli as a host, and produced 26kDa of protein. Further analysis of the enzyme showed that the enzymeis thermostable. In addition, the enzymewas purified through Ion Metal Affinity Chromatography and it showed as single band with the homogeneity at around 96%.
机译:通过宏基因组学方法从印度尼西亚西爪哇的Domas Crater分离出一种新颖的II类醛缩酶。该酶的序列分析与来自未培养的嗜酸丝孢菌的古细菌核糖5-磷酸4-表异构酶高度同源。同一性百分比为63%。对该蛋白质的同源性分析表明,该蛋白质序列包含II类醛缩酶的所有保守基序。该酶与其他醛缩酶一样显示出Zn2 +结合,多肽结合和活性位点。对该酶的系统发生分析表明,该酶形成了一个不同的分支,该分支与未发酵的Acilolosbus sp。的核糖5-磷酸4-表异构酶关闭。该基因在大肠杆菌中作为宿主表达,并产生26kDa的蛋白质。对该酶的进一步分析表明该酶是热稳定的。此外,该酶通过离子金属亲和色谱法纯化,显示为单条带,均质性约为96%。

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