巴氏醋酸杆菌AS1.41产醋酸关键酶研究  

Study on the key enzymes of acetic acid production from Acetobacter pasteurianus AS1.41

作　　者：陈洋[1] 高冰[1] 汪超[1] 李冬生[1] 徐宁[1] 胡勇[1] 

机构地区：[1]湖北工业大学工业发酵湖北省协同创新中心湖北省食品发酵工程技术研究中心,湖北武汉430068

出　　处：《中国酿造》2016年第1期38-42,共5页China Brewing

基　　金：湖北省自然科学基金(2015CFB678);湖北省级教育部门青年人才项目(Q20151412)

摘　　要：巴氏醋酸杆菌(Acetobacer pasteurianus)将乙醇氧化成醋酸的关键酶是乙醇脱氢酶(ADH)和乙醛脱氢酶(ALDH)。在不同初始乙醇含量条件下,ADH和ALDH的酶活呈现动态变化,乙醇含量为4%时,ADH和ALDH的酶活达到最大,分别为7.43 U/mg和7.18 U/mg。同时,酶活与产酸速率呈现出较高一致性:酶活越高,产酸速率越快。发酵温度为32℃时,菌体生长最为活跃,酶活最大,产酸最快;加入0.5%的乙酸后,ADH和ALDH的酶活分别由8.12 U/mg和7.06 U/mg提高到了9.43 U/mg和8.52 U/mg,产酸速率也得到相应提升。ALDH对乙醇、乙酸、温度的稳定性均高于ADH。The alcohol dehydrogenase （ADH） and aldehyde dehydrogenase （ALDH） were the key enzymes which ethyl alcohol was oxidized into acetic acid by Acetobacter pasteurianus. The enzyme activity of ADH and ALDH presented dynamic changes under the conditions of different initial ethanol content. When ethanol content was 4%, the enzyme activity of ADH and ALDH reached the maximum 7.43 U/mg and 7.18 U/mg, respectively. Enzyme activity and acid production rate presented a high consistency. The higher the enzyme activity, the faster the acid produces. When the fermentation temperature was 32℃, the growth of the strain was the most active; the enzyme activity reached to the highest, and the acid production rate was the fastest. After adding acetic acid 0.5%, the enzyme activity of ADH and ALDH increased from 8.12 U/mg and 7.06 U/mg to 9.43 U/mg and 8.52 U/mg, respectively. Acid production rate was also improved. The stability of ALDH on ethanol, acetic acid, and temperature was higher than that of ADH.

关 键 词：巴氏醋酸杆菌 乙醇脱氢酶 乙醛脱氢酶 乙醇 温度 乙酸 

分 类 号：TS264.2[轻工技术与工程—发酵工程]