Abstract
A novel species of alkaliphilic Bacillus (JAMB-602), isolated from a soil sample, was found to exoproduce an alkaline mannanase. The mannanase gene was cloned by the shotgun method and sequenced. Its open reading frame encodes a protein of 490 amino acids with a calculated molecular mass of 53,763 Da. The deduced amino acid sequence showed similarity to those of known mannanases in glycoside hydrolase family 5, with only 32-58% identity. The recombinant mature enzyme with a molecular mass of 50 kDa was hyper-exoproduced with Bacillus subtilis as the host, corresponding to a level of approximately 2 g/L. The homogeneously purified enzyme had a molecular mass of 50 kDa, an optimal temperature of 65°C, and an optimal pH of around 9. It was thermostable with a half-life of 2 h at 55°C. N-Bromosuccinimide abolished the enzymatic activity. The pattern of mannan hydrolysis showed that the enzyme is an endo-type mannanase.
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