摘要
以醋醅中筛选出产α-淀粉酶的酵母菌为出发菌进行N+离子注入诱变,使产物酶活提高了219%,达到497U/g。对其所产-α淀粉酶进行分离纯化,实验表明,该酶的最适温度为60℃,最适pH值为4.0,分子量约为81kDa,Ca2+对该酶的激活作用不明显。薄层层析结果表明,该酶水解淀粉产物为糊精和多种低聚糖。
The α-amylase producing yeast, which was screened from solid-substrate fermented vinegar, was mutated by nitrogen ion beam injection technique. The activity of acid α-amylase was increased 497 U/g. The acid α-amylase was purified and analyzed. It was indicated that the optimum temperature and pH of the acid α-amylase were 60℃ and 4.0 respectively, and the molecular weight of the enzyme was about 81 kD. The Ca^2＋ could not affect the activity of the acid α-amylase remarkably. From thin-layer chromatography, it was shown that oligosaccharide and dextrin were produced from starch by the catalysis of acid α-amylase.
出处
《中国酿造》
CAS
北大核心
2007年第1期10-13,共4页
China Brewing
