Multifunctional α-amylase Amy19 possesses agarase, carrageenase, and cellulase activities.

The open reading frame of an α-amylase coding gene, amy19, was obtained from a fosmid genomic library of hot spring bacterium Bacillus BI-19 by a plate-based assay of carrageenase activity. After heterologous expression of the gene, the recombinant Amy19 was found to possess α-amylase, agarase, carrageenase, and cellulase activities, and could degrade soluble starch, agarose, carrageen, and sodium cellulose into oligosaccharides with low degrees of polymerization. To explore the multifunctional mechanism of Amy19, three continuous glycosyl hydrolase 70 (GH70) motifs in the Amy19 encoding sequence were deleted one by one, then in pairs, then all at once. The GH70 motifs may play an important role in the multifunctionality of Amy19, but the multifunctionality was not determined by the GH70 motifs alone. To our knowledge, this is the first report of an α-amylase from a hot spring bacterium with additional agarase, carrageenase, and cellulase activities.