Fig. 2
Biochemical characterization of different laminarinases from Formosa B. Michaelis–Menten Kinetic (a) of FbGH30 on native laminarin, b of FbGH17A on native and debranched laminarin and c of FbGH17B on debranched laminarin (native laminarin is illustrated by the solid lines and debranched laminarin by the dashed lines). d Visualization of all three enzymatic activities was done using HPAEC-PAD. FbGH30 hydrolyzed native laminarin. After this debranching reaction, the laminarin was purified to remove glucose for the following steps. This debranched laminarin was used in the FbGH17A reaction. FbGH17B hydrolyzed the products of the previous FbGH17A reaction without any further purification in between. e 3D structure model of both the MFS-domain and the associated FbGH17B-domain and its potential arrangement within the inner-membrane. The modeling was performed using Phyre2. f The overall structure of FbGH17A is displayed in cyan with the additions colored purple. Highlighted in red are the catalytic residues. The N- and C-termini are labeled. g A surface view of FbGH17A with a modeled substrate complex shown as sticks in yellow from a GH17 transferase of Rhizomucor miehei with laminaritriose and laminaribiose in the −3 to −1 and + 1 to + 2 subsites, respectively
