In this study, the gene encoding an alpha-amylase from a psychrophilic Arthrobacter agilis PAMC 27388 strain was cloned into a pET-28a(+) vector and heterologously expressed in Escherichia coli BL21(DE3). The recombinant alpha-amylase with a molecular mass of about 80 kDa was purified by using Ni2+-NTA affinity chromatography. This recombinant alpha-amylase exhibited optimal activity at pH 3.0 and 30 A degrees C and was highly stable at varying temperatures (30-60 A degrees C) and within the pH range of 4.0-8.0. Furthermore, alpha-amylase activity was enhanced in the presence of FeCl3 (1 mM) and beta-mercaptoethanol (5 mM), while CoCl2 (1 mM), ammonium persulfate (5 mM), SDS (10 %), Triton X-100 (10 %), and urea (1 %) inhibited the enzymatic activity. Importantly, the presence of Ca2+ ions and phenylmethylsulfonyl fluoride (PMSF) did not affect enzymatic activity. Thin layer chromatography (TLC) analysis showed that recombinant A. agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, producing maltose as the major end product. These results make recombinant A. agilis alpha-amylase an attractive potential candidate for industrial applications in the textile, paper, detergent, and pharmaceutical industries.