Biochemical and Enzymatic Properties of a Novel Marine Fibrinolytic Enzyme from Urechis unicinctus

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Abstract

A novel potent protease, Urechis unicinctus fibrinolytic enzyme (UFE), was first discovered by our laboratory. In this study, we further investigated the enzymatic properties and dynamic parameters of UFE. As a low molecular weight protein, UFE appeared to be very stable to heat and pH. When the temperature was <50°C, the remnant enzyme activity remained almost unchanged, but when the temperature was raised to 60°C the remnant enzyme activity began to decrease rapidly. UFE was quite stable in a pH range of 3.0–12.0, especially at slightly alkaline pH values. Mn2+, Cu2+, and Fe2+ ions were activators of UFE, whereas Fe3+ and Ag+ ions were inhibitors. Fe2+ ion along with Fe3+ ion might regulate UFE activity in vivo. The optimum pH and temperature of UFE were about 8.0 and 50°C, respectively. When using casein as substrate and a substrate concentration <0.1% casein (w/v), the reaction velocity was increased with substrate concentration. Also when using casein as substrate, the determined Km and Vmax of UFE were 0.5298 mg/mL and 3.0845 mol of L-tyrosine equivalent, respectively. Our systematic research results are significant when UFE is applied for medical and industrial purposes.

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