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Heterologous expression and characterization of novel 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) from Pyrobaculum calidifontis and Meiothermus ruber
- Lou, Xiao-cong, Zheng, Cheng-cai, Chen, Wen-qi, Ma, Yuan-xin, Mkingule, Idefonce, He, Fei-fan, Fei, Hui
- Process biochemistry 2019 v.80 pp. 35-42
- Escherichia coli, Meiothermus ruber, acetaldehyde, catalytic activity, fructose-bisphosphate aldolase, genes, heterologous gene expression
- To overcome the deficiency in which 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) exhibits low levels of catalytic efficiency in aldol reactions and poor tolerance for high concentrations of aldehyde, two novel deoC genes encoding DERAPyc and DERAMet were identified in Pyrobaculum calidifontis and Meiothermus ruber that had heterologous expression in E. coli BL21. The specific activities toward 2-Deoxy-d-ribose-5-phosphate (DR5P) of DERAPyc and DERAMet were 13.6 ± 0.1 and 85.2 ± 0.7 U/mg, respectively. Almost 56.2% (DERAPyc) and 21.7% (DERAMet) of their activity remained after being incubated for 6 h in 300 mM acetaldehyde at 25℃. In addition, the DR5P concentration in the reaction catalyzed by DERAPyc and DERAMet was almost 0.31 and 2.63 times the amount catalyzed by DERAEco after reacting for 6 h, respectively. These results suggest that these two novel DERAs with a high tolerance for a high concentration of aldehyde have the potential to be widely used in industrial settings.