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罗非鱼鳃组织中脂肪氧合酶的性质研究 被引量:21

Characterization of a Lipoxygenase From Nile Tilapia Gills
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摘要 试验结果表明脂肪氧合酶最适反应温度为30℃,最适pH为10.0和4.0。在pH10.0的条件下,最适底物浓度为2.5×10-4mol/L,Km值为0.073mmol/L,Vmax值为3.08×104U/mgprotein.min。EDTA对该酶有较强的抑制作用。而在pH4.0的条件下,最适底物浓度为5×10-4mol/L,BHA、BHT、TBHQ等抗氧化剂有较强的抑制作用。 Characterization of a lipoxygenase were carried out from Nile tilapia Oreohromis niloticus gills. The results showed that the enzyme had optimal temperature of 30℃,and optimal pH of 10.0 and 4.0. There were at least two isoforms in this enzyme. The optimal substrate concentration was 2.5×10 -4 mol/L at pH 10.0, and Km and Vmax were 0.073 mmd/L and 3.08×104 U/mg protein.min, respectively. EDTA was a better inhibitor. The optimal substrate concentration was 5×10 -4 mol/L for the lipoxygenase activity at pH 4.0. Anti-oxidants such as butylhydroxyanisol (BHA), butylated hydroxyl toluene (BHT) and TBHQ had strong inhibit effects.
出处 《水产科学》 CAS 北大核心 2005年第7期15-19,共5页 Fisheries Science
关键词 脂肪氧合酶 罗非鱼 lipoxygenase Nile tilapia Oreohromis niloticus gill characterization
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