Properties of glutelin from mature and developing rice grain

Villareal, Ruth M.; Juliano, Bienvenido O.

doi:10.1016/s0031-9422(00)94141-4

Cited by 66 publications

(31 citation statements)

References 9 publications

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“…1 and 4). Juliano et al reported that the 16-kD subunits, which seems to correspond to the 13-kD peptide in our experiment (26), is the major component at the 4-to 7-DAF stages in the cultivars IR 26 and IR 480-5-9, and that only traces of the 25-and 38-kD subunits of glutelin are present (29). In contrast, our results showed that the 13-kD peptide appeared at later stages than the 22-to 23-and 37-to 39-kD peptides, the smaller peptides of the storage protein being synthesized later than the larger peptides.…”

Section: And B)supporting

confidence: 57%

“…(25) demonstrated that it has a heterogeneous mol wt. The increase in glutelin in the developing rice grain coincides with the appearance of PB' in the starchy endosperm 7 to 8 DAF (7,29), and glutelin is found exclusively in PB (7,26,30). In a previous paper (26), we reported two types of PB in the starchy endosperm of rice grains and described their isolation.…”

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confidence: 68%

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Biosynthesis of Storage Proteins in Developing Rice Seeds

Yamagata

Sugimoto²,

Tanaka³

et al. 1982

Plant Physiol.

289

203

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Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the starchy endosperm protein of rice (Oryza sativa L. Japonica cv Koshihikari) during seed development confirmed that storage protein begins to accumulate about 5 days after flowering. Two polypeptide groups, 22 to 23 and 37 to 39 kilodaltons, the components of glutelin, the major storage protein in rice seed, appeared 5 days after flowering. A 26-kilodalton polypeptide, the globulin component, also appeared 5 days after flowering. Smaller polypeptides (10-to 16-kilodaltons) including prolamin components, appeared about 10 days after flowering. In contrast, the levels of the 76-and 57-kilodalton polypeptides were fairly constant throughout seed development. Transmission electron microscopy and fractionation by sucrose density gradient centrifugation of the starchy endosperms at various stages of development showed that protein body type II, the accumulation site of glutelin and globulin, was formed faster than protein body type I, the accumulation site of prolamin.The 57-kilodalton polypeptide but not the glutelin subunits was labeled in a 2-hour treatment with I14CIleucine given between 4 and 12 days after flowering to developing ears. In vivo pulse-chase labeling studies showed the 57-kllodalton polypeptide to be a precursor of the 22 to 23 and 37 to 39 kilodalton subunits. The 57-kilodalton polypeptide was salt-soluble, but the mature glutelin subunits were almost salt insoluble.In vitro protein synthesis also showed that the mRNAs directly coding the 22 to 23 and 37 to 39 kilodalton components were absent in developing seeds and that the 57-kilodalton polypeptide was the major product. Thus, it was concluded that the two subunits of rice glutelin are formed through post-translational cleavage of the 57-kilodalton polypeptide.The major storage proteins of most cereal grains are glutelin and prolamin. In rice grains, however, glutelin is the major protein of the starchy endosperm, constituting at least 80%o of the total protein, prolamin accounting for less than 5% (12). Rice glutelin has a mol wt of 6 x I05 according to Tecson et al. (27), but Takeda et a!. (25) demonstrated that it has a heterogeneous mol wt. The increase in glutelin in the developing rice grain coincides with the appearance of PB' in the starchy endosperm 7 to 8 DAF (7,29), and glutelin is found exclusively in PB (7,26,30). In a previous paper (26), we reported two types of PB in the starchy endosperm of rice grains and described their isolation. One (type I, PB-I) is spherical with a concentric ring structure, whereas the other (type II, PB-II) is stained homogeneously by osmium tetroxide and does not have this structure. PB-I contains prolamin, and PB-II is rich in glutelin and globulin. The glutelin in PB-II is composed of two principal subunits, the 22-to 23-and 37-to 39-kD complexes, and the prolamin in PB-I is composed mainly of 13-kD polypeptide.

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Section: And B)supporting

confidence: 57%

mentioning

confidence: 68%

Biosynthesis of Storage Proteins in Developing Rice Seeds

Yamagata

Sugimoto²,

Tanaka³

et al. 1982

Plant Physiol.

289

203

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 96%

“…Concerning the differences between the Japonica and Indica samples, slightly higher lysine and lower tyrosine seems to characterize the latter. This evidence could be related to the higher protein content in Indica which is positively correlated to the glutelin fraction; in particular, a higher lysine and glutamic acid content and lower tyrosine is typical of the major fraction extracted in iso-propanol-β-mercaptoethanol (Villareal and Juliano, 1978).Protein digestibility The milling process is able to remove some external components such as anti nutritional factors, the phytic acid and protease inhibitors from the kernel. As a consequence, in milled rice, the palatability and protein digestibility (PD) greatly increases.…”

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confidence: 99%

Nutritional and Physicochemical Characterisation of Italian Rice Flours and Starches

Acquistucci

Francisci

Bucci

et al. 2009

FSTR

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Six Japonica and three Indica rice samples were considered in this study. Total amino acid composition and protein digestibility were studied in relation to protein component while, amylose content, resistant and damaged starch were considered to assess starch characteristics. Results showed a comparable amino acid pattern and carbohydrate but different protein and starch digestibility. Due to the different botanical origin of samples, the amylose content raged between 15.5 and 25.2 g/100 g d. b. to whom corresponded a wide range of pasting temperatures determined by means of Differential Scanning Calorimetry. Principal Component Analysis, used to perform an exploratory data analysis, evidenced the contribution of some amino acids in recognising samples and this evidence could be usefully employed in breeding programs.Keywords: milled rice, nutrient availability, Italian rice, thermal analysis *To whom correspondence should be addressed. E-mail: acquistucci@inran.it IntroductionRice is the staple food for half of the world's population. It is currently the most rapidly growing food source in Africa. The rice proteins are rich in glutelins and have relatively high lysine content when compared to other grains. Rice is generally easily digested and absorbed by humans producing high glycemic response; however, genetic characteristics and technological processes can reduce the availability to the enzymic degradation so reducing the glycemic response (Casiraghi et al., 1993).There are more than 20 species of rice (Oryza genus) but only two species, O. sativa and O. glaberrima, offer an agriculture interest for humans. Among different varieties, there is a wide variability for grain shape, size, amyloseamylopectin content and endosperm colour and, although rice is cultivated worldwide (about 100.000 varieties), there is no universal rice quality attribute even though cooked rice texture represents one of the main quality factors. Concerning the nutritional properties, cultivar-specific differences in nutrients content, cultural practices as well as post harvest activities can be responsible for loss of nutrients. For this reason, nutrients content should be among the main criteria used in the selection of rice cultivars for use in areas of food insecurity (Fresco, 2005).Italy is the main rice producer in EU. However, Italian exporters have to face the increasingly competition of other rice exporting countries. Some difficulties for Italian rice exporters are due to the fact that traditionally cultivated rice types do not always suit the taste of the consumer from Central and Northern Europe: therefore, to meet customers' requirements, breeding programmes are in progress to produce indica-type varieties, long and not sticky, as an alternative to the so called Japonica-type (long or short but bold sized types) traditionally cultivated.The first goal of the present paper was to provide additional data on the physicochemical and nutritional properties of rice flours and corresponding starch of some Italian rice varieties i...

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“…The loss of protein from brown rice during milling ranged from 11.0 to 26% at milled rice recoveries of 86-90% and it was found that high protein rice offered greater resistance to milling by standard methods. Glutelin (alkali or acid soluble proteins) account for 80% or more of the total seed protein and thus the principal protein of whole grain (brown and milled rice), while albumin and globulin were the major proteins in rice bran (Cagampang et al, 1966;Juliano, 1972;Villareal and Juliano, 1978). Refined milling of successive layers of brown rice has revealed that the second outermost 5% fraction had the highest level of protein (Hogan et al, 1964).…”

mentioning

confidence: 99%