摘要
通过硫酸铵分级沉淀、SephadexG5 0凝胶层析和DEAE Sepharose阴离子交换层析 ,从米曲霉 3 0 42中提取得到了米曲氨基酰化酶 ,该酶的纯化倍数为 5 4.2 9,比活为 647.66U/mg ,总收率为49 5 3 %。详细考察了温度、pH、缓冲体系的离子强度和金属离子对米曲氨基酰化酶酶活的影响。结果表明 ,该酶促反应的最适pH为 7 5～ 8 0 ,最适反应温度随催化反应时间的延长而降低 ,缓冲体系中的离子对酶活有抑制作用 ,而低浓度的Co2 +对酶活有激活作用。
The aminoacylase from Aspergillus oryzae 3042 was partially purified by ammonium sulfate fractionation, Sephadex G50 and DEAE-Sepharose cloumn chromatography. The specific activity of aminoacylase was 647.66*#U/mg. The purification ratio and recovery was 54.29 and 49.53% respectively. The optimal pH of the aminoacylase was 7.5～8.0, and with the increase of catalysis time, the optimal reaction temperature decreased correspondingly. The ions in the buffer lowered the activity of aminoacylase, but the Co 2+ in low concentration activated the aminoacylase.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2004年第3期36-41,共6页
Food and Fermentation Industries
基金
国家自然科学基金资助项目 (No .2 0 2 76 0 6 5 )
