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Inhibition of cyclodextrins on α-galactosidase
Di Yao1, Zhenzhou Zhu2, Hongyan Cai2
1School of Food Science and Technology, Wuhan Polytechnic University, Wuhan 430023, China.
Abstract:
This work successfully investigated the effects of different influential factors and hydrophobic cavities of cyclodextrins (CDs) on α-galactosidase (α-Gal) by detecting α-Gal activity. The highest inhibitory concentration of three kinds of CDs (α-, β-, and γ-CD) on α-Gal was 10mM. Moreover, the highest inhibition of α-Gal was obtained under the following conditions: reaction time of 90min, temperature of 30°C, and pH 6.0. Compared with other CDs, β-CD showed more ability to interact with α-Gal due to its appropriate cavity geometric dimensions. From circular dichroism and nuclear magnetic resonance it was observed that β-CD changed the secondary structure of α-Gal and formed a hydrogen bond with this enzyme.
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