摘要
提取酵母菌中的碱性磷酸酶,并对其性质做出分析。结果显示酶促反应最适pH值为10.3,初速度V0=0.01367μmol/L.min,以对硝基苯磷酸二钠(pNPP)为底物测得Km=0.535mmol/L、Vm=0.01429μmol/L。较低浓度的Mg2+对酶有较强的促进作用,2mmol/L时达到641%,磷酸氢二钠对碱性磷酸酶有竞争性抑制作用。
Alkaline phosphatase was extracted and purified from yeast which was prepared by the culturing the dusty yeast and the biochemical characterization were investigated. The results showed that the optimum pH was 10.3 for the hydrolysis of pNPP. The initial velocity is 0.01367 μ mol/L·min. The Michaelis-Menten constant （Km） is 0.535 mmol/L and the maximun velocity （Vm） is 0.01429 μ mol/L at pH10.1 and 37℃. The Mg^2＋ ion with the concentration of 2mmol/L could increase the enzyme activity by 541%, implying that low concentration of Mg^2＋ could enhance the activity of the enzyme significantly. Na2HPO4 could inhibit the enzyme activity and the inhibition was found to be of competitive type.
出处
《安徽农学通报》
2008年第8期93-95,共3页
Anhui Agricultural Science Bulletin
关键词
酵母菌
碱性磷酸酶
酶的性质
酶促反应
Yeast
Alkaline phosphatase
Enzyme activity
Enzymatic reaction
