Recombinant expression, purification, and characterization of an α-amylase from .

This work reports the 1 gene cloning from CTI-57, and its successful expression in Rosetta™ (DE3) from the pTRCHis2B plasmid. The recombinant AMY1 protein had 47 kDa, and its modeled structure showed a monomer composed of three domains. An -terminal domain with the characteristic (β/α)-barrel structure of α-amylases, which contained the catalytic amino acid residues.