Functional analysis of alpha-1,3-glucanase: the enzyme participates in fungal cell-wall hydrolysis

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Bacillus circulans KA-304 alpha-1,3-glucanase (Agl-KA) is a multi-domain enzyme, and it includes N-terminal DS1, CB6, DS2, UCD, and C-terminal catalytic domain. To clarify the role of these domains, we constructed several domain deletion enzymes and GFP-fusion proteins. As the results, DS1, CB6, and DS2 domain bound to alpha-1,3-glucan and fungal cell-wall, and that binding efficiency was increased by combined action. The findings indicate that DS1, CB6, and DS2 are novel alpha-1,3-glucan binding domain.In order to obtain the further information on structure and function of alpha-1,3-glucanases, we purified and characterized a novel alpha-1,3-glucanase (Agl-FH1) of Paenibacillus glycanilyticus FH11. Although the properties of Agl-FH1 were almost the same as those of Agl-KA, the amino acid sequence of catalytic domain of Agl-FH1 showed approximately 20% identity to that of Agl-KA. The results may be beneficial to clarify the catalytic mechanism of the enzyme in the future.