摘要
对高产蛋白酶细菌P5菌株发酵产生的蛋白酶进行初步分离纯化并研究其酶学性质。结果表明,硫酸铵饱和度为70%时,酶活性达到最高(310.44U/mL);该酶最适反应温度为40℃,在35～40℃保温5h,酶活性基本没变化;酶反应最适pH值为7.0,酶活性在pH值6.0～7.5时比较稳定。K+、Ca2+、Mg2+、Fe3+对酶活性有促进作用,Na+对酶活性基本没有影响,Hg2+和Mn2+对酶活性有抑制作用,其他金属离子对酶活性的影响随离子浓度的不同而不同。
The protease produced by a bacterium strain P5 was purified with ammonia sulfate,and the characteristics of this enzyme was investigated.The results showed that the enzymatic activity of the protease was the highest activity（310.44 U/mL） when the concentration of ammonia sulfate is 70%.The enzyme had an optimum pH of 7.0 and temperature of 40 ℃,at the same time,it was stable in pH 6.0-7.5 and temperature of 35-40 ℃,respectively.Under the determined test condition,K＋,Ca2＋,Mg2＋,Fe3＋ could improve the enzyme activity;Na＋ had no effect on enzymatic activity of the protease;whereas,Hg2＋,Mn2＋ inhibited the enzyme activity;other metal ions have different effects on enzyme activity according to their concentration.
出处
《西北农业学报》
CAS
CSCD
北大核心
2012年第4期164-167,共4页
Acta Agriculturae Boreali-occidentalis Sinica
基金
中国博士后基金(2011M501431)
国家自然科学基金(31071722)
山西省软科学(2010041031-02)
关键词
蛋白酶
纯化
酶学性质
Proteinase
Purification
Enzymatic characteristics
