Salt-activated endoglucanase of a strain of alkaliphilic Bacillus agaradhaerens.

An endoglucanase was purified to homogeneity from an alkaline culture broth of a strain isolated from seawater and identified here as Bacillus agaradhaerens JAM-KU023. The molecular mass was around 38-kDa and the N-terminal 19 amino acids of the purified enzyme exhibited 100% sequence identity to Cel5A of B. agaradhaerens DSM8721(T).

Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme.

A novel alkaline mannanase Man26A has been found in the culture of an alkaliphilic Bacillus sp. strain JAMB-750 and the optimal pH for the mannanase activity of the enzyme was around pH 10 (J Biol Macromol 4: 67-74, 2004). This optimal pH is the highest among those of the mannanases reported to date.

Crystallization and preliminary X-ray study of alkaline mannanase from an alkaliphilic Bacillus isolate.

An alkaline mannanase (EC 3.2.1.