In Vivo Digestibility of Rice Prolamin/Protein Body-I Particle Is Decreased by Cooking

Rice has storage proteins, e.g., glutelin, globulin and prolamin, in the seeds, which are used as nitrogen sources during germination. Rice prolamin has been reported to be an indigestible protein that decreases the nutritional value of rice. However, the causes for the indigestibility of prolamin are currently not clear. The objective of this study was to determine if prolamin is naturally indigestible or if cooking affects its digestibility. The gastrointestinal (GI) transit of rice 23 kDa glutelin (23G) and 13 kDa prolamin (13P) in Wistar/ST rats fed raw rice (RR) and cooked rice (CR) diets was assessed using Western blot analysis. We also measured the excretion of these proteins in the feces of these rats. Additionally, morphological observation of the structure of type-I protein bodies in the feces was performed using electron microscopy. Assessment of GI transit revealed that 23G rapidly disappeared from the GI contents of both the RR and CR groups, but 13P accumulated in the cecum of the CR group. In the CR group, prolamin, maintaining the structure of PB-I, was fully excreted in the feces. These results indicate that rice prolamin is not indigestible by nature, but is rendered indigestible by cooking.