Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions.
Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions.
复制标题
极端条件下具有高结构稳定性的氢化醋微菌酶的酯酶活性表征。
DOI:
10.1007/s00792-018-1038-3
复制
发表时间:
2018
期刊:
影响因子:
--
通讯作者:
Kumagai PS
中科院分区:
文献类型:
--
作者:
Kumagai PS
The biotechnological and industrial uses of thermostable and organic solvent-tolerant enzymes are extensive and the investigation of such enzymes from microbiota present in oil reservoirs is a promising approach. Searching sequence databases for esterases from such microbiota, we have identified in silico a potentially secreted esterase fromAcetomicrobium hydrogeniformans, named AhEst. The recombinant enzyme was produced inE. colito be used in biochemical and biophysical characterization studies. AhEst presented hydrolytic activity on short-acyl-chainp-nitrophenyl ester substrates. AhEst activity was high and stable in temperatures up to 75 °C. Interestingly, high salt concentration induced a significant increase of catalytic activity. AhEst still retained ~ 50% of its activity in 30% concentration of several organic solvents. Synchrotron radiation circular dichroism and fluorescence spectroscopies confirmed that AhEst displays high structural stability in extreme conditions of temperature, salinity, and organic solvents. The enzyme is a good emulsifier agent and is able to partially reverse the wettability of an oil-wet carbonate substrate, making it of potential interest for use in enhanced oil recovery. All the traits observed in AhEst make it an interesting candidate for many industrial applications, such as those in which a significant hydrolytic activity at high temperatures is required.