Molecular species in the protein body II (PB-II) of developing rice endosperm.

SUGIMOTO, Toshio; Tanaka, Kunisuke; Kasai, Zenzaburo

doi:10.1271/bbb1961.50.3031

Cited by 19 publications

(5 citation statements)

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“…which are extremely insoluble in water [6][7][8][9]. Furthermore, because of the presence of lipid, which is easily hydrolyzed by lipase or oxidized causing rancidity in rice, rice bran needs to be stabilized such as by heat or acid treatment to deactivate the lipase or by defatting to remove the lipid [10][11][12].…”

Section: Rice Bran 21 Bran Proteinmentioning

confidence: 99%

“…Rice proteins are extremely insoluble because of intermolecular disulfide linkages and high molecular weights of the major protein glutelin [6][7][8][9]. The solubility and other food-use functional properties are further reduced during processing, particularly by modifications such as heat treatment for bran stabilization [18,[38][39][40].…”

Section: Processing On Functional Propertiesmentioning

confidence: 99%

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An update on the processing of high‐protein rice products

Shih¹

2003

Nahrung

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The component of protein in rice, at 7-9% by weight, is relatively low, but the total amount of rice protein potentially available is significant because the production of rice worldwide, at 380 million tons annually, is huge. Rice proteins are recognized as nutritional, hypoallergenic, and healthy for human consumption, and rice protein products have been in demand in recent years. However, because of difficulties in the processing, rice protein products, particularly high-protein content ones, have not been readily available. Two of the main sources of rice protein, rice bran and, to a lesser extent, broken rice kernels, have been under-used and under-priced. This report provides an update on the processing of these sources for rice proteins. Methods of protein processing are highlighted including the traditional alkaline extraction, enzyme-assisted extraction, and the novel uses of physical treatment prior to water extraction. Also discussed are effects of processing on the functional and nutritional properties of rice protein.

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Section: Rice Bran 21 Bran Proteinmentioning

confidence: 99%

Section: Processing On Functional Propertiesmentioning

confidence: 99%

An update on the processing of high‐protein rice products

Shih¹

2003

Nahrung

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“…The glutelin polypeptides are synthesized on the endoplasmic reticulum (ER) membrane as a precursor form (proglutelin) of 57 kilodaltons (kD) (Yamagata et al 1982). Within the ER, proglutelin forms one or more intracellular disulfide bond (SatohCruz et al 2010a), is glycosylated (Kishimoto et al 1999), and assembles to form a tetramer (Sugimoto et al 1986) before it is exported from the ER to the PSVs (Krishnan et al 1986, Yamagata and, where it is posttranslationally processed to acidic and basic subunits in PSV (Yamagata et al 1982). These subunits are bounded together by an interchain disulfide bond and are accumulated as a hexamer in the PSV (Kumamaru et al 2010, Sugimoto et al 1986).…”

Section: Introductionmentioning

confidence: 99%

“…Within the ER, proglutelin forms one or more intracellular disulfide bond (SatohCruz et al 2010a), is glycosylated (Kishimoto et al 1999), and assembles to form a tetramer (Sugimoto et al 1986) before it is exported from the ER to the PSVs (Krishnan et al 1986, Yamagata and, where it is posttranslationally processed to acidic and basic subunits in PSV (Yamagata et al 1982). These subunits are bounded together by an interchain disulfide bond and are accumulated as a hexamer in the PSV (Kumamaru et al 2010, Sugimoto et al 1986). The alcohol-soluble prolamins, the second most abundant storage protein in rice, are also synthesized on the ER but are then sequestered within this compartment to form PB-I.…”

Section: Introductionmentioning

confidence: 99%

Gene-gene interactions between mutants that accumulate abnormally high amounts of proglutelin in rice seed

et al. 2010

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We had previously identified eight mutants, esp2 and g(G)lups1 to 7, which accumulated abnormally high amounts of proglutelin, the major storage protein in rice seeds. Analysis of their seed proteins by SDS-PAGE, their levels of the luminal chaperone BiP and gene-gene interactions indicated that these mutants fell into four classes. The most epistatic class consisted of esp2, which encodes a defective protein disulfide isomerase (PDI). A second class consisting of Glup1, glup2 and glup7 was hypostatic to esp2, and showed abnormally high levels of BiP, suggesting that maturation and export of proglutelins from the ER are inhibited in this class of mutants. The third class containing glup4, Glup5 and glup6 mutations was hypostatic to esp2, Glup1, glup2 and glup7. Since the glup4 allele encodes the small GTPase Rab5a, which participates in the trafficking of proglutelin from Golgi apparatus to the protein storage vacuole (PSV), this third class of mutants is likely affected in this process. Lastly, glup3, which encodes a vacuolar processing enzyme, which proteolytically processes proglutelin into acidic and basic subunits within the PSV, was hypostatic to the other mutants. Overall, these gene relationships are consistent with the sequential intracellular transport and processing of proglutelin and provide novel insights on the trafficking of proglutelin to the PSV.

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“…The precursors are then transported via the Golgi complex to the vacuole, and are proteolyticaly cleaved to generate acidic (37-39kDa) and basic subunits (22-23 kDa) [3,4]. During seed maturation, glutelins accumulate in type II protein bodies (PB-II) which derive from the vacuole [5], and the glutelin subunits assemble into polymers through inter-molecular disulfide bond formation [6]. An Asn-Gly dipeptide is conserved as the post-translational cleavage site in 11S legumin-like storage proteins from dicotyledon and monocotyledon plants.…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning of a Novel Glutelin cDNA from Rice Seeds.

Mitsukawa

Hayashi

Yamamoto

et al. 1998

Plant Biotechnology

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A novel glutelin gene was cloned from a cDNA library of maturing rice seeds (Oryza sativa L. cv Nipponbare) . The 2.0kbp insert contained an open reading frame encoding a 510 amino acid polypeptide (Mr 57,116). This novel glutelin shares 46 to 49% amino acid identity with previously identified rice glutelins. A phylogenetic analysis of cloned glutelins indicates that this gene constitutes a new, fifth class of glutelin gene families. The Asn-Gly processing sequence which is highly conserved in 11S seed storage proteins is replaced by Asn-Val in the sequence of the novel glutelin. The amino acid composition extending 50 residues both upstream and downstream of the Asn-Val site was less hydrophilic than in other glutelins. The N-terminal half corresponding to the acidic domains of other glutelins possesses a higher pI value (7.46) than found in other glutelins. Expression of the gene was detected in maturing seeds, but not in roots or leaves.

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Molecular species in the protein body II (PB-II) of developing rice endosperm.

Cited by 19 publications

References 0 publications

An update on the processing of high‐protein rice products

An update on the processing of high‐protein rice products

Gene-gene interactions between mutants that accumulate abnormally high amounts of proglutelin in rice seed

Molecular Cloning of a Novel Glutelin cDNA from Rice Seeds.

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