四川农业大学学报 ›› 2011, Vol. 29 ›› Issue (03): 391-391.

• 研究论文 • 上一篇    下一篇

野生荞麦籽粒中芦丁降解酶的分离纯化

唐宇1,邵继荣2,罗庆林1,郑亚迪2,孙俊秀3   

  1. 1.
    2. 四川农业大学
    3. 四川烹饪高等专科学校
  • 收稿日期:2011-06-20 修回日期:2011-08-15 出版日期:2011-09-30 发布日期:2011-10-13
  • 通讯作者: 邵继荣
  • 基金资助:

    荞麦野生种质资源的保护和利用研究;苦荞异黄酮代谢途径关键酶基因的克隆

Purification of rutin degrading enzyme from wild buckwheat kernels

  • Received:2011-06-20 Revised:2011-08-15 Online:2011-09-30 Published:2011-10-13
  • Contact: SHAO Jirong

摘要:

从野生荞麦种金荞麦籽粒中提取出芦丁降解酶,具有将芦丁降解为槲皮素的作用。该粗酶液用葡聚糖凝胶柱G-100和DEAE阴离子交换柱分离纯化后,最终酶的比活性由59.2 U/mg提高到671.4U/mg,纯化倍数和回收率分别为11.3倍和3.5%。所得酶液经SDS-PAGE检测酶分子量大小为60kDa左右。对酶液反应条件进行研究,发现酶的最适温度为40℃,最适pH值为5.0。在工业生产上可借助芦丁降解酶以酶解法取代酸解法生产槲皮素。

关键词: 野生荞麦, 金荞麦, 芦丁降解酶, 槲皮素, 芦丁

Abstract:

The rutin degrading enzyme which was extracted from seeds of Fagopyrum cymosum, one of wild buckwheat species, could effectively degrade rutin into quercetin. The rutin-degarding enzyme was purified with Sephadex G-100 and DEAE cellulose-32 anion exchange column. The enzyme was purified to 11.3-fold with 3.5% recovery, and the specific activity increased from 59.2 U/mg to 671.4 U/mg. SDS-PAGE analysis revealed a single protein band corresponding to a molecular mass of 60 KDa. Maximum enzyme activity was obtained at 40℃ and pH 5.0. Based on the results in this study, the rutin-degrading enzyme has great potential to replace the classical acid-hydrolytic method to produce quercetin in industrial application.

Key words: wild buckwheat, Fagopyrum cymosum, rutin degrading enzyme, quercetin, rutin