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首页> 外文期刊>Biotechnology Progress >Characterization of Recombinant Glyoxylate Reductase from Thermophile Thermus thermophilus HB27
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Characterization of Recombinant Glyoxylate Reductase from Thermophile Thermus thermophilus HB27

机译：嗜热嗜热菌HB27重组乙醛酸还原酶的表征

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摘要

A glyoxylate reductase gene from the thermophilic bacterium Thermus thermophilus HB27 (TthGR) was cloned and expressed in Escherichia coli cells. The recombinant enzyme was highly purified to homogeneity and characterized. The purified TthGR showed thermostability up to 70 °C. In contrast, the maximum reaction condition was relatively mild (45 °C and pH 6.7). Although the k_(cat) values against co-enzyme NADH and NADPH were similar, the K_m value against co-enzyme NADH was ～18 times higher than that against NADPH. TthGR prefers NADPH rather than NADH as an electron donor. These results indicate that a phosphate group of a co-enzyme affects the binding affinity rather than the reaction efficiency, and TthGR demands appropriate amount of phosphate for a high activity. Furthermore, it was found that the half-lives of TfhGR in the presence of 25% dimethyl sulfoxide and diethylene glycol were significantly longer than that in the absence of an organic solvent.
机译：克隆了嗜热嗜热菌HB27（TthGR）的乙醛酸还原酶基因，并在大肠杆菌细胞中表达。将重组酶高度纯化至均质并进行表征。纯化的TthGR在高达70°C的温度下显示出热稳定性。相反，最大反应条件是相对温和的（45°C和pH 6.7）。尽管针对辅酶NADH和NADPH的k_（cat）值相似，但针对辅酶NADH的K_m值比针对NADPH的K_m值高约18倍。 TthGR更喜欢NADPH而不是NADH作为电子供体。这些结果表明，辅酶的磷酸根基团影响结合亲和力而不是反应效率，并且TthGR需要适当量的磷酸根以实现高活性。此外，发现在存在25％二甲基亚砜和二甘醇的情况下，TfhGR的半衰期明显长于在不存在有机溶剂的情况下的TfhGR的半衰期。

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