Synergism for xylo-oligosaccharides, ρ-coumaric and ferulic acid production, and thermostability modulation of GH 62 α-l-arabinofuranosidase

GH 62 α-L-arabinofuranosidases are a group of enzymes that preferably hydrolyze l-arabinose residues of arabinoxylans. Albeit the least studied, these enzymes have gained attention because they exert synergistic action with other xylanolytic enzymes for arabinoxylan depolymerization. This is the first study on the thermodynamic and kinetic parameters, structural prediction, and metal ion effect on the thermostability of a GH 62 arabinofuranosidase subfamily 1. The optimum enzymatic conditions are pH 4.8 and 42 °C, and the presence of Ca2+ and Mn2+ ions enhanced the thermostability and activity. The synergism of this arabinofuranosidase with a GH 10 endoxylanase increased the production of xylo-oligosaccharides 2.3 times with additional coproduction of 0.82 mM of ferulic acid and 0.09 mM of ρ-coumaric acid released from corn hull arabinoxylan (4% w/v). These results are relevant to developing an enzymatic formulation that is economically feasible for industrial applications, especially for prebiotic and antioxidant compounds production in the food and pharmaceutical sectors from sources rich in arabinoxylan, especially agro-industrial wastes of grains husks and peels.