Seed Structure and Localization of Reserves inChenopodium quinoa

Abstract

The three areas of food reserves in quinoa seeds are : a large central perisperm, a peripheral embryo and a one to twocell layered endosperm surrounding the hypocotyl-radicle axis of the embryo. Cytochemical and ultrastructural analysis revealed that starch grains occupy the cells of the perisperm, while lipid bodies, protein bodies with globoid crystals of phytin, and proplastids with deposits of phytoferritin are the storage components of the cells of the endosperm and embryo tissues. EDX analysis of the endosperm and embryo protein bodies revealed that globoid crystals contain phosphorus, potassium and magnesium. These results are compared with studies on other perispermous seeds published to date.

Distribution of Minerals in Quinoa (Chenopodium quinoaWilld.) Seeds

“…Similar observations have been previously reported. 5,6) In this study, we found that Ca occurred mostly in the pericarp and seed coat as well as in the boundary between perisperm and embryo (Fig. 1).…”

“…In quinoa seeds, it has been observed that phytin globoids are included in protein bodies of embryonic cells and that P, Mg, and K are localized in the globoids with energy dispersive X-ray (EDX) analysis. 5,6) These analyses, however, were done by point analysis which involves analyzing areas of the size of the electron beam. In the aspect of mineral nutrition, we need the information of the overall distribution of mineral nutrients in whole quinoa seeds.…”

“…These observations were similar to that of seeds of Amaranthus, 10) taxonomically close to Chenopodium. By a point EDX analysis, P, K, and Mg have been detected in carbon-coated embryonic tissues 5) or the globoid crystals obtained from powdered preparation of embryonic tissues 6) of quinoa. Prego et al 6) concluded that P, K, and Mg are component of the phytin globoid crystals within protein bodies and that X-ray intensities of the three elements were not significantly different between cotyledon and hypocotyl-radicle axis.…”

Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

“…Likewise, the rice prolamins are isolated in Type I protein bodies (Saito et al, 2012) and the glutelins are isolated in Type II protein bodies (Yamagata et al, 1982) and in oats the globulin and prolamin storage proteins are co-located in the same protein bodies (reviewed by . The albumin and globulin storage proteins of the pseudocereals, amaranth (Coimbra and Salema, 1994), buckwheat (Elpidina et al, 1990) and quinoa (Prego et al, 1998) are also isolated in protein bodies. The localisation of storage proteins in discrete protein bodies in these "gluten-free" grains is unlike the situation in wheat where the glutenin and gliadin proteins form a continuous matrix around the starch granules within the cells of the mature starchy endosperm (reviewed by .…”

A Hybrid Dry and Aqueous Fractionation Method to Obtain Protein-Rich Fractions from Quinoa (Chenopodium quinoa Willd)

“…For quinoa seeds (~15 w/dw% protein), it is extremely difficult to separate protein bodies from starch granules as these are similar in size (Prego et al 1998). However, quinoa protein bodies are concentrated in the embryo of the seed (~23.5 w/dw% protein), while starch granules are concentrated in the perisperm (Ando et al 2002).…”