Recombinant chimeric alpha-amylase (AmyP-Cr) was constructed by a catalytic core of alpha-amylase (AmyP) from a marine metagenomic library and a starch-binding domain (SBDCr) of alpha-amylase from Cryptococcus sp. S-2. The molecular fusion did not alter optimum pH, optimum temperature, hydrolysis products, and an ability of preferential and rapid degradation towards raw rice starch, but catalytic efficiency and thermostability were remarkably improved compared with those of the wild-type AmyP. AmyP-Cr achieved the final hydrolysis degree of 61.7 +/- 1.2% for 10% raw rice starch and 47.3 +/- 0.8% for 15% raw rice starch after 4 h at 40 A degrees C with 1.0 U per mg of raw starch. The catalytic efficiency was very high, with 3.6-4.0 times higher than that of AmyP. The enhanced catalytic efficiency was attributed to the better thermostability and the higher adsorption and disruption to raw rice starch caused by SBDCr. The properties of AmyP-Cr open a new way in terms of a new design of raw rice starch processing.