The hydrolysis of sodium pyrophosphate (TSPP) in the fresh Aristichthys nobilis minced meat was studied by using ion chromatography (IC) in this work. The biochemical properties of the crude pyrophosphatase (Ppase) were also be studied. The results showed that TSPP was hydrolyzed to orthophosphate (Pi) in A. nobilis minced meat. There was a resoluble pyrophosphatase in the A. nobilis meat. The optimum temperature and pH for the crude PPase activity of A. nobilis meat was 50 ℃, and 8.0, respectively. The PPase activity was activated by Mg²⁺, Mn²⁺ and Co²⁺, but Mg²⁺ was the more suitbale to the crude PPase. Under the condition of 1 mol·L^-1 Mg²⁺, the PPase activity was 0.023 μmol·min^-1·mg^-1. Glucose 6-phosphate (G-6-P) could inhibit the activity of crude PPase. The crude PPase activity was activated under the condition of below 1 mol·L^-1 EDTA-Na₂, but was consumingly inhibited when the concentration of EDTA-Na₂ over 1 mol·L^-1.