20619350
not annotated - annotated - LINNAEUS only
Characterization of the GPI-anchored endo Beta-1,3-glucanase Eng2 of Aspergillus fumigatus.
A GPI-anchored endo Beta-1,3-glucanase of Aspergillus fumigatus was characterized. The enzyme encoded by ENG2 (AFUA_2g14360) belongs to the glycoside hydrolase family 16 (GH16). The activity was characterized using a recombinant protein produced by Pichiapastoris. The recombinant enzyme preferentially acts on soluble Beta-1,3-glucans. Enzymatic analysis of the endoglucanase activity using Carboxymethyl-Curdlan-Remazol Brilliant Blue (CM-Curdlan-RBB) as a substrate revealed a wide temperature optimum of 24-40^0C, a pH optimum of 5.0-6.5 and a K(m) of 0.8 mg ml(-1). HPAEC analysis of the products formed by Eng2 when acting on different oligo-Beta-1,3-glucans confirmed the predicted endoglucanase activity and also revealed a transferase activity for oligosaccharides of a low degree of polymerization. The growth phenotype of the Afeng2 mutant was identical to that of the wt strain.
Ann file
T1 Species 69 90 Aspergillus fumigatus
N1 Reference T1 Taxonomy:746128
T2 Species 136 157 Aspergillus fumigatus
N2 Reference T2 Taxonomy:746128
T3 Species 343 357 Pichiapastoris
N3 Reference T3 Taxonomy:4922