Analysis of alpha-amylase inhibitor from corni fructus by coupling magnetic cross-linked enzyme aggregates of alpha-amylase with HPLC-MS
文献类型: 外文期刊
第一作者: Cen, Yin
作者: Cen, Yin;Liu, Fang;Yu, Jingang;Jiang, Xinyu;Chen, Xiaoqing;Liu, Liangliang
作者机构:
关键词: alpha-Amylase;Corni fructus;Cross-linked enzyme aggregates;HPLC-MS;Magnetic
期刊名称:JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES ( 影响因子:3.205; 五年影响因子:3.068 )
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收录情况: SCI
摘要: As a carrier-free immobilization strategy, magnetic cross-linked enzyme aggregates (MCLEAs) showed improved enzyme activity, stability and magnetic response. In this study, MCLEAs of a-amylase (MCLEAs amylase) was prepared under optimized conditions and characterized with scanning electron microscope and vibrating sample magnetometer. The prepared MCLEAs amylase showed an amorphous structure and the saturation magnetization was 33.5 emu/g, which was sufficient for magnetic separation. Then MCLEAs amylase coupled with high performance liquid chromatography mass spectrometry (HPLC MS) was utilized to screen and identify a-amylase inhibitors from ethyl acetate extract of corni fructus. The experiment conditions were optimized. At the optimum conditions (incubation time: 10 min, pH: 7.0 and temperature: 20 degrees C), querciturone was successfully screened and identified with weak nonspecific binding. The screening result was verified by inhibition assays and the IC50 value of querciturone was 22.5 mu g/mL. This method provided a rapid way to screen active compounds from natural products. (C) 2015 Elsevier B.V. All rights reserved.
分类号: Q503
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