Analysis of α-amylase inhibitor from corni fructus by coupling magnetic cross-linked enzyme aggregates of α-amylase with HPLC-MS.
J Chromatogr B Analyt Technol Biomed Life Sci
; 995-996: 64-9, 2015 Jul 15.
Article
em En
| MEDLINE
| ID: mdl-26038235
ABSTRACT
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 α-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 33.5emu/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 α-amylase inhibitors from ethyl acetate extract of corni fructus. The experiment conditions were optimized. At the optimum conditions (incubation time 10min, pH 7.0 and temperature 20°C), querciturone was successfully screened and identified with weak non-specific binding. The screening result was verified by inhibition assays and the IC50 value of querciturone was 22.5µg/mL. This method provided a rapid way to screen active compounds from natural products.
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Base de dados:
MEDLINE
Assunto principal:
Extratos Vegetais
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Cornus
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Inibidores Enzimáticos
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Enzimas Imobilizadas
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Alfa-Amilases
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article