4 methylumbelliferone 4 mub

All the enzyme assays were performed on a microplate at 25 °C and a pH of 7 with 700 μL of the phosphate buffer-soluble fraction extracted from the bast fibers (Fig. S1). All the enzyme activities were expressed as nmol g -1 dry bast tissue h -1 . The cellobiohydrolase, β-D-glucosidase, β-D-xylosidase, β-D-galactosidase and α-L-arabinosidase activities were assayed in three replicates with the release of the fluorogenic product 4-methylumbelliferone (4-MUB, Sigma-Aldrich, Germany) according to a method adapted from Bell et al. (2013) (link) as previously described by Sauvadet et al. (2016) (link). The polygalacturonase activity was quantified in duplicate by measuring the reducing end groups formed during the enzymatic degradation of polygalacturonic acid (0.5 g L -1 ) using 3,5dinitrosalicylic acid (DNS) reagent (Miller, 1959) (link) and a galacturonic acid calibration curve. After 1 h of incubation, the reaction was stopped by adding 500 μL of dinitrosalicylic acid. The solutions were then boiled in water for 15 min. The absorbance of the solution was measured at 510 nm using a microplate spectrophotometer (Versamax, Molecular Devices, USA).