Classification, Substrate Specificity and Application of α-Galactosidases

Abstract

Galactose is found in many oligosaccharides, galactomannans, glycoproteins and glycolipids, which are widely distributed in plants microorganisms and animals. α-Galactosidase (α-Gal) catalyzes the hydrolysis of 1,6-linked α-galactosyl residues and transgalactosylation. α-Gals are classified into four glycoside hydrolases families (GH): 4, 27, 36 and 57. The majority of known α-Gals belongs to GH families 27 and 36.α-Gals are of particular interest in view of their biotechnological applications.

Identification and Characterization of a Thermostable GH36 α-Galactosidase from Anoxybacillus vitaminiphilus WMF1 and Its Application in Synthesizing Isofloridoside by Reverse Hydrolysis

“…The optimal pH of galV was found to be approximately 7.5, which was consistent with the previous finding that GH36 enzymes functioned optimally at neutral or alkaline pH [ 20 ]. Figure 5 shows that galV manifested the maximum activity at 60 °C, which was in agreement with the α-galactosidase from Paceilomyces thermophila [ 19 ] and higher than that reported for α-galactosidase from Bifidobacterium breve (37 °C) [ 21 ] and Aspergillus oryzae YZ1 (50 °C) [ 22 ].…”

Magnetic Nanoparticles Coated with Thiomannosides or Iminosugars to Switch and Recycle Galactosidase Activity

“…We selected the DNJ ligands to be grafted at Fe 3 O 4 MNPs , as we previously showed significant AgaB activation with soluble DNJ‐coated dextrans . Mannosides were also selected to obtain control SMan@Fe 3 O 4 1 with similar properties to 2 but with potentially different electrostatical behavior and inability to interact in the AgaB binding site . Interestingly, gold NPs and nanodiamonds coated with O ‐glycosides were shown to be stable towards matching glycosidase hydrolysis , .…”