Biochemical and structural characterization of Penicillium purpurogenum α-D galactosidase: Binding of galactose to an alternative pocket may explain enzyme inhibition

Recombinant production and characterization of six novel GH27 and GH36 α-galactosidases from Penicillium subrubescens and their synergism with a commercial mannanase during the hydrolysis of lignocellulosic biomass

“…In contrast, seven putative α-galactosidases were found in GH36 with only one protein containing a secretory signal peptide. This high number of extracellular GH27 proteins compared to those of GH36, has been observed previously in other fungi, where most extracellularly active α-galactosidases belong to GH27, while a small portion belong to GH36 (Ademark et al, 2001b;Bauer et al, 2006;Morales-Quintana et al, 2017;Nakai et al, 2010). This has been suggested to have evolutionary origin, being caused horizontal transfer of GH27 AGLs from eukaryotes to bacteria, while the opposite may have occurred for GH36 AGLs (Naumoff, 2004).…”

Three-Phase Partitioning of α-Galactosidase from Aspergillus lentulus: Optimization of System and Characterization of Enzyme

“…KM from other fungal α-galactosidases ranging from 0.11 to 11 mM. This indicate that the enzyme has high affinity towards the PNPG [20,22,23].…”

“…P. purpurogenum α-galactosidase have an optimum at 50°C. It is also compared with other fungal α-galactosidases [20]. As most the fungal enzymes have high temperature optimums (50-75°C) and thermostability (40-70°C) for various times [20,37].…”

“…Inhibitory effect and kinetics of galactose on partitioned α-galactosidase D-Galactose is also an inhibitor of α-galactosidases from microbial sources [20,24,38]. The effect of various concentrations (0.25-10 mM) of galactose on α-galactosidase activity was assayed.…”

“…They catalyze the hydrolysis of α-linked terminal non-reducing galactose residues from galactose oligosaccharides, galactomannans and galactolipids. α-Galactosidases have find various industrial applications such as in su-gar industry to increase the yield of crystallized sugar, in feed industry as an animal feed additive to improve nutritional value, in pulp and paper industry to improve pulp bleaching and also in clinical applications such as for the treatment of Fabry's disease by enzyme replacement therapy and to convert B blood group to O blood group [20][21][22]. α-Galactosidases have been purified from different microbial sources with a number of purification protocols including salting-out, ion-exchange, affinity chromatography etc [23][24][25].…”