摘要
采用 (NH4 ) 2 SO4 盐析、SephadexG 2 0 0凝胶过滤和ConA Sepharose亲和层析方法对蒜氨酸酶进行了部分纯化 ,并研究了其酶动力学特性 ,结果表明其最适反应温度为 3 0℃ ,最适pH值为6 2 4,以蒜氨酸为底物 ,最大反应速度Vmax =1 2 0u/mg(蛋白质 ) ,米氏常数 Km =6 0 2× 1 0 - 3mol/L。
After partial purification of alliinase with 40%～55% saturation (NH 4) 2SO 4,G-200 Sephadex and ConA-sepharose affinity chromatography, the kinetic characteristics of alliinase were studied. The result showed that the optimal temperature is 30℃and pH is 6.24. Maximum velocity is 120units/mg of protein and Michaelis constant is 6.02×10 -3mol/L. The research also showed that the cation irons (Ca 2+, Mg 2+, Zn 2+ and Fe 2+) have activation effect and Cu 2+, L-cysteine has inhibition effect on the activity of alliinase.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2004年第9期1-4,共4页
Food and Fermentation Industries
基金
国家自然科学基金 (No .C0 2 0 2 10 0 5 )
国家"86 3"计划 (No.2 0 0 1AA2 4 80 2 1)资助
