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Updated: Jun 23, 2025
Author Spotlight: Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
Published on: June 2, 2023
Optimization of High-Activity earthworm fibrinolytic enzyme extraction methods and protein component analysis
Zhihui Zhao1, Zhiyuan Liu1, Qiyao Jiang1
1School of Life Sciences, Beijing University of Chinese Medicine, Beijing 102488, China.
Objective:
Optimize the extraction process of earthworm fibrinolytic enzyme.
Methods:
Chinese common earthworms underwent a series of purification processes, including grinding, salting out, hydrophobic medium chromatography, ammonium sulfate precipitation, and ion exchange chromatography, to obtain purified earthworm fibrinolytic enzyme.
Results:
Utilizing Pheretima aspergillum as the starting material, we discovered that the specific activity of lumbrokinase extracted via ammonium sulfate precipitation was 58 U/mg, noticeably surpassing that achieved through heat precipitation and ethanol precipitation methods. After undergoing two rounds of chromatographic separations employing hydrophobic affinity chromatography and anion exchange chromatography, the specific activity of the lumbrokinase protein soared to 9267 U/mg, significantly exceeding the 3,178 U/mg specific activity attained through industrial extraction methods.
Discussion:
The development of a novel crude extraction method for lumbrokinase protein can significantly boost its activity and purity. The discovery of a high-efficiency purification method and the identification of protein components within highly active lumbrokinase pave the way for further investigations into these proteins.
