ENERGY-DISPERSIVE X-RAY-ANALYSIS OF PHYTIN GLOBOIDS IN ALEURONE PARTICLES OF DEVELOPING RICE GRAINS

In this study energy-dispersive X-ray analysis was used to discover changes in the composition of phytin globoids in aleurone particles of developing rice grains. At early milky stage (the 7th to 10th day after flowering) many aleurone particles were observed as electron lucent vacuole-like particles in aleurone cells, some of which contained a small electron-dense inclusion (phytin globoid). The major mineral elements present in phytin globoids were phosphorus (P) and magnesium (Mg). Potassium (K) was also detectable but its concentration was extremely low relative to these two. Calcium (Ca) and zinc (Zn) were found as minor components. At early dough stage (the 17th to 19th day after ftowering) P, Mg and K were observed as the major mineral elements. The composition of mineral elements in phytin globoids tend to be constant in the late staae of ripening. On the other hand, minor elements, i.e. Ca and Zn, were only detectable in the early stage of ripening, suuesting that these elements accumulated in the aleurone particles only during the early stage, and in later stage their accumulation was either complete or at very low levels compared with those of K and Mg. The relative amount of Mg existing in phytin globoid remained roughly constant throughout the ripening periods, while that of K varied. Energy-dispersive X-ray analysis of phytin globoids in developing rice aleurone particles confirmed that the accumulation of P, Mg and K in rice grains was closely related to the formation of phytin globoids. This analysis suggested further that the mechanism of accumulation of P into aleurone particles was very similar to that of Mg, while that of K differed from both. The results obtained suggested that Ca and Zn might be required in the formation of phytin globoid at the early ripening stage. EDX analysis of a protein body in the starchy endosperm revealed that there was no significant element detectable in an EDX spectrum other than sulfur. This suggests that lamellar concentric structures in protein bodies are not due to phytin. © 1979 Taylor & Francis Group, LLC.