植物学报 ›› 2005, Vol. 22 ›› Issue (05): 579-583.

• 实验简报 • 上一篇    下一篇

新鲜大蒜中蒜氨酸酶的分离纯化及性质

李燕 王荣 李冠 苟萍   

  1. (新疆大学生命科学与技术学院 乌鲁木齐 830046)
  • 收稿日期:2004-01-07 修回日期:2004-04-19 出版日期:2005-10-30 发布日期:2005-10-30
  • 通讯作者: 苟萍

Purification and Properties of Alliinase from Fresh Garlic (Allium sativum)

LI Yan WANG Rong LI Guan GOU Ping   

  1. (College of Life Science and Technology, Xinjiang University, Urumqi 830046)
  • Received:2004-01-07 Revised:2004-04-19 Online:2005-10-30 Published:2005-10-30
  • Contact: GOU Ping

摘要: 用葡聚糖凝胶G-200层析柱分离纯化了新鲜大蒜(Allium sativum)中的蒜氨酸酶, SDS-PAGE结果为单一条带, 分子量为53 kD在35 ℃下以蒜氨酸为底物, Km为0.693 mmol.L-1, Vmax 为0.353 mmol.min-1, 最适反应温度为30 ℃, 热稳定的温度在50 ℃以下。Zn2+对酶有抑制作用, Mn2+使酶活力增加。

Abstract: Alliinase (EC.4.4.1.4) of fresh garlic (Allium sativum) was purified 14-fold by gel filtration on a SephadexG-200 system. SDS-PAGE revealed a molecular weight of 53 kD, with Km and Vmax values of 0.693 mmol.L-1 and 0.353 mol.L-1, respectively. The optimal temperature for activity was 30 ℃, with stable activity below 50 ℃. The activity was inhibited by Zn2+ stimulated by 0.1 mol Mn2+.