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WANG Dianliang,LIU Wanshun,HAN Baoqin. 2007. Enzymatic properties of UFE, a novel marine fibrinolytic enzyme. Acta Oceanologica Sinica, (2):84－93
Enzymatic properties of UFE, a novel marine fibrinolytic enzyme
Enzymatic properties of UFE, a novel marine fibrinolytic enzyme
Received:April 03, 2006  Revised:August 28, 2006
DOI：
Key words:marine animal  fibrinolytic enzyme  protease  enzyme properties
中文关键词:  marine animal  fibrinolytic enzyme  protease  enzyme properties
基金项目:
Author NameAffiliationE-mail
WANG Dianliang College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China  
LIU Wanshun College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China wanshunliu@hotmail.com 
HAN Baoqin College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China  
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Abstract:
      A novel potent protease, Urechis unicinctus fibrinolytic enzyme (UFE), was firstly discovered.The enzymatic properties of UFE were further investigated.As a low molecular mass protein, UFE appeared to be very stable to heat and pH.When temperature was below 50℃, the remnant enzyme activity remained almost unchanged, but when temperature was raised to 60℃, the remnant enzyme activity began to decrease rapidly.UFE was quite stable in the range of pH value from 3 to 12, especially in slightly alkaline pH value.Mn2+, Cu2+ and Fe2+ ions were activators of UFE, while Fe3+ and Ag+ ions were inhibitors of UFE.Fe2+ ion along with Fe3+ ion might regulate UFE activity in vivo.The optimum pH and temperature of UFE were about 8 and 50℃, respectively.Other characteristics of this enzyme were also studied.Systematic research results are significant when UFE is applied for medical and industrial purposes.
中文摘要:
      A novel potent protease, Urechis unicinctus fibrinolytic enzyme (UFE), was firstly discovered.The enzymatic properties of UFE were further investigated.As a low molecular mass protein, UFE appeared to be very stable to heat and pH.When temperature was below 50℃, the remnant enzyme activity remained almost unchanged, but when temperature was raised to 60℃, the remnant enzyme activity began to decrease rapidly.UFE was quite stable in the range of pH value from 3 to 12, especially in slightly alkaline pH value.Mn2+, Cu2+ and Fe2+ ions were activators of UFE, while Fe3+ and Ag+ ions were inhibitors of UFE.Fe2+ ion along with Fe3+ ion might regulate UFE activity in vivo.The optimum pH and temperature of UFE were about 8 and 50℃, respectively.Other characteristics of this enzyme were also studied.Systematic research results are significant when UFE is applied for medical and industrial purposes.
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