Extracellular ${alpha}$-amylases produced by a newly isolated feather degrading bacterium strain Bacillus mojavensis A21 was optimized and characterized. Zymography showed that the A21 strain produced at least two ${alpha}$-amylases. Higher ${alpha}$-amylase production was achieved in the presence of 10 g/L chicken feathers and 1 g/L yeast extract. The growth of B. mojavensis A21 using chicken feathers as the nitrogen and carbon source resulted in its complete degradation after 48 h incubation at $37^{circ}C$. However, maximum ${alpha}$-amylase activity was attained after 24 h. The optimum temperature and pH for crude ${alpha}$-amylase activity were $60^{circ}C$ and 6.5, respectively, and its activity was inhibited by EDTA. The end products of starch hydrolysis were maltose, maltotriose, and maltotetraose. ${alpha}$-Amylases from the A21 strain also catalyzed transglycosylation reactions when maltotetraose and maltopentaose were used as substrates and formed higher molecular weight maltoligosaccharides from G5 to G8. The maltooligosaccharide forming endo-${alpha}$-amylases is useful in bread making as an anti-staling agent and can be produced economically using a low-cost medium with chicken feathers as the substrate.