Inhibition of cyclodextrins on α-galactosidase

Food Chem. 2017 Feb 15:217:59-64. doi: 10.1016/j.foodchem.2016.08.057. Epub 2016 Aug 21.

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.

Keywords: cyclodextrin; inhibition; α-Galactosidase.

MeSH terms

  • Circular Dichroism
  • Cyclodextrins / chemistry*
  • Cyclodextrins / pharmacology*
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Temperature
  • alpha-Galactosidase / antagonists & inhibitors*

Substances

  • Cyclodextrins
  • alpha-Galactosidase