C-terminal domain of beta-1,3-glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble beta-1,3-glucan

Abstract

The deduced amino acid sequences of 72-kDa beta-1,3-glucanase from Bacillus circulans WL-12 (GIcA) and 91-kDa enzyme from B. circulans IAM1165 (BglH) are highly homologous, except that the latter has an additional long C-terminal region composed of 192 amino acid residues. Two mutant enzymes (BgIH deprived of the C-terminal region and GIcA with the C-terminal region added) were constructed. The enzymes possessing the C-terminal region bound more abundantly to pachyman (insoluble beta-1,3-glucan) and A.spergillus oryzae cell wall than those not possessing the region. This indicates that the C-terminal region participated in binding of the enzymes to insoluble beta-1,3-glucan.