A Comparison of the Transglycosylation Capacity between the Guar GH27 Aga27A and Bacteroides GH36 BoGal36A α-Galactosidases

The transglycosylation behavior and capacity of two clan GH-D α-galactosidases, BoGal36A from the gut bacterium Bacteroides ovatus Aga27A guar plant, was investigated compared. enzymes were screened for ability to use para-nitrophenyl-α-galactoside (pNP-Gal), raffinose locust bean gum (LBG) galactomannan as glycosyl donors with acceptors methanol, propanol, allyl alcohol, propargyl alcohol glycerol using mass spectrometry. was, in general, more stable presence acceptors. HPLC analysis developed used a second screening method reactions or LBG donor substrate propanol Time-resolved set up methanol acceptor, respectively, order develop an insight into basic properties, including ratio between rate (methyl galactoside synthesis) hydrolysis. had somewhat higher (0.99 compared 0.71 Aga27A) at early time points but indicated be prone secondary (product) hydrolysis prolonged incubations. methyl yield when (48% 38% (27% 30% Aga27A).