A chimeric enzyme, engineered from two rice cc-amylase isozymes, Amy1A and Amy3D, showed unique characteristics in soluble-starch and maltoheptaose hydrolysis. Effects of pH on soluble-starch hydrolysis and the thermostability of the chimeric enzyme were similar to those of the isozyme Amy3D. The previous study revealed that Amy1A shows high activity in soluble-starch hydrolysis and low activity in oligosaccharide degradation, while Amy3D shows low activity in soluble-starch hydrolysis and high activity in oligosaccharide degradation. The chimeric enzyme showed high activities in both soluble-starch hydrolysis and oligosaccharide degradation. These results suggest that protein modules of highly homologous enzymes are interchangeable, and that a novel enzyme with unique characteristics can be obtained by creating a chimeric enzyme.