A novel lipase from Aspergillus oryzae catalyzed resolution of (R,S)-ethyl 2-bromoisovalerate
A novel lipase from Aspergillus oryzae catalyzed resolution of (R,S)-ethyl 2-bromoisovalerate
复制标题
一种来自米曲霉的新型脂肪酶催化拆分 (R,S)-2-溴异戊酸乙酯
作者：
Wu Peng;Zhang Mengjie;Zhang Yinjun;Wang Zhao;Zheng Jianyong
在本研究中，源自米曲霉 WZ007 的新型脂肪酶 M5 易于表现出高水解活性和对外消旋底物 (R,S)-2-溴异戊酸乙酯的立体选择性。通过酶法拆分得到(R)-2-溴异戊酸乙酯，它是高效对映体氟胺氰菊酯的关键手性中间体。结果表明，酶促反应在120mM外消旋底物中进行3小时，对映体过量达到98.6%，转化率为51.7%，E值在120以上。因此，新型脂肪酶M5具有高效生产(R)-2-溴异戊酸乙酯的能力，大大降低了氟胺氰菊酯高效对应物的工业化生产成本。
In this study, a novel lipase M5 derived fromAspergillus oryzaeWZ007 was prone to exhibit high hydrolytic activity and stereoselectivity towards racemic substrate (R,S)‐ethyl 2‐bromoisovalerate. (R)‐ethyl 2‐bromoisovalerate was obtained by enzymatic resolution, which is the key chiral intermediate for highly efficient enantiomerically fluvalinate. The results showed that the enzymatic reaction was carried out in 120mM racemic substrate for 3 hours, the enantiomeric excess reached 98.6%, the conversion was 51.7%, andEvalue above 120. Therefore, the novel lipase M5 has the ability to efficiently produce (R)‐ethyl 2‐bromoisovalerate, which greatly reduces the industrial production cost of the highly efficient counterpart of fluvalinate.