Skip to main content
Fig. 4 | Biotechnology for Biofuels and Bioproducts

Fig. 4

From: Characterization of two 1,3-β-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-β-glucan metabolism of fungal saprotrophs

Fig. 4

Scheme of the reaction catalyzed by 1,3-β-transglucanase ΔG7048 using LAM5 as a substrate, and degradation of the product(s) by exo-1,3-β-glucanase G9376. Top panel: hydrolysis catalyzed by exo-1,3-β-glucanase G9376 on LAM5 as deduced from the analyses shown in Figs. 1d, 2 and Additional File 2: Fig. S3. Bottom panel: transglycosylation catalyzed by 1,3-β-transglucanase ΔG7048 using LAM5 as substrate, and subsequent hydrolysis of the hybrid octamer(s) by exo-1,3-β-glucanase G9376. Red line indicates the putative 1,6-β-glycosidic linkage. The molar ratio of degradation products obtained from both enzymatic reactions (2xLAM5 + G9376) and (2xLAM5 + ΔG7048 + G9376) are reported on the right. The reducing end (R) of each LAM5 oligomer is also indicated [Glc D-Glucose, LAM2 laminaribiose, LAM3 laminaritriose, LAM5 laminaripentaose; Y, residue n. 6 or n. 7 or n. 8]

Back to article page