• Applied Biological Chemistry
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• v.32 no.1
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• pp.64-72
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• 1989

Near full length cDNA clones encoding the rice seed storage protein, prolamine, were isolated and divided into two homology classes based on cross-hybridization and DNA sequencing analysis. These cDNA clones contain a single open reading frame encoding a putative rice prolamine precursor(M.W.=17,200) possessing atypical 14 amino acid signal peptide. Clones of these two homology classes diverge mainly by insertions/deletions of short nucleotide stretches and point mutations. The deduced primary structures of both types of prolamine polypeptides are devoid of any major tandem repetitive sequences, a feature prevalent in other cereal prolamines. No significant homology teas detected between the rice prolamine and other cereal prolamines, indicating that the rice gene evolved from a different ancestor that gave rise to other cereal prolamine genes. Developing wheat and rice endosperms were examined using ultrathin sections prepared from tissues harvested at various days after flowering. By immunocytochemical localization techniques, wheat prolamines are localized within vesicles from Golgi apparatus and in homogeneous regions of protein bodies. The involvement of the goli apparatus in the packaging of wheat prolamines into protein bodies indicates a pathway which differs from the mode of other cereal prolamines and resembles the mechanism employed for the storage of rice glutelin and legume globulins.

• Journal of Plant Biology
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• v.36 no.4
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• pp.327-335
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• 1993

The active sites, intracellular transport, function of cellulase in association with the disintegration of the storage materials of the endosperm cells during seed maturation and after-ripening of Panax ginseng C.A. Meyer seeds were studied by electron microscopy. Cytochemical activities of the cellulase occurred in protein bodies and vesicles of endosperm cells in seed with red seed coat. In after-ripening seed, the activities were strongly found in the cell wall of endosperm near the umbiliform layer and on neighbouring vesicles, so it is assumed that these cells begin to be decomposed. Cellulase activities were initiated before the decomposition of storage materials. But, no activity was observed in the umbiliform layer, so it is suggested that cellulase lose its activity after the completion of lysis process.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.6
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• pp.564-570
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• 1994

This experiment was conducted to determine seed storage protein pattern and structural character of differed peanut cultivars during germination. Soluble protein content in both Namdae and Daekwang cultivars remarkably decreased in cotyledon site at 2 or 3 days after incubation(DAI) and in embryonic axis site at 1 or 2 DAI, showing 28∼29% in cotyledon site and 10% in embryonic axis site at 5 DAI. Protein subunits such as 66, 43, 40 and 35.5kD bands in the cotyledon site of Namdae and Daekwang cultivars disappeared, but 21.5-23kD band disappeared slightly, but low polypeptide band such as 14-16kD increased gradually, and the same trend has been obserbed in embryonic axis site during 2 DAI. The amount of new protein formed during germination period was highest in cotyledon site at 3 DAI, and in embryonic axis site at 2 DAI. 16kD bend detected in cotyledon site of Daekwang cultivar during germination.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.47
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• pp.163-174
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• 2002

Peanut is one of the principal oil seeds in the world as a rich source of edible oil and protein. Peanut quality arises as a result of a complex interaction of genetic, physiological and biochemistry processes that produce the chemical composition of the peanut seed. The major factors influencing seed quality are degree of maturity and digging and drying, curing and storage as a series of harvesting. The end products, peanut butter, salted seed, confections, roasting stock and by-products are favored in world-wide because of their unique roasted peanut flavor, Literatures are reviewed mainly focusing on the physiological properties and nutritional quality of oil, protein and flavor in peanut. Chemical properties of protein and oil, and volatile flavor component in peanut seeds are studied. The objectives of this paper were to review and summarize the results obtained from the improving quality breeding program and evaluation of the chemical composition in peanut up to now.

• Journal of Plant Biology
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• v.37 no.3
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• pp.293-299
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• 1994

Developing rice endosperm cells display two morphologically distinct rough endoplasmic reticulum (ER) membranes, the cisternae ER (C-ER) and theprotein body ER (PB-ER), the latter delimiting the prolamine protein bodies. We (Li et al., 1993) have recently shown that the storage protein mRNAs are not randomly distributed on these ER types; the C-ER is enriched for glutelin mRNAs, whereas the PB-ER harbors predominantly prolamine transcripts. To address whether these ER types have differnet capacities to translate these mRNAs and translocate their proteins into the lumen, a microsomal fraction enriched in C-ER vesicles was prepared from devleoping rice seeds. When present in an in vitro translatin system, the microsomes were able to proteolytically remove the signal peptide and internalize both preproglutelin and preprolamine within the microsomal vesicles. Of the two species, preprolamine was more effectively translocated and processed. These results suggest that the C-ER has the capacity to recognize and bind both storage protein mRNAs during protein synthesis. Moreover, efficient translocation and processing of glutelin requires additional factors that are deficient or absent in the in vitro system.

• Korean Journal of Agricultural Science
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• v.24 no.2
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• pp.121-125
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• 1997

A total of 437 landraces of rice from Vietnam were analyzed for total seed protein by SDS-PAGE and phenol reaction. The different types of glutelin $\alpha$ subunits were detected. The level of wx protein with 60kDa molecular weight was divided into 3 groups, corresponding to non-glutinous, intermediate and glutinous starch types. Based on the variation in seed storage protein and wx protein, landraces were classified into 7 groups. Frequency distribution of types A and B of glutelin $\alpha$ subunits changed with the latitude at which rice landraces were collected. Geographical cline for phenol reaction was detected.

• Food Science of Animal Resources
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• v.36 no.3
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• pp.300-308
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• 2016

In this study, the effects of grape seed flour on the physical-chemical properties, microbiological and sensory properties of Turkish dry fermented sausage, sucuk, was investigated. After the sausages produced with beef, beef fat, sheep tail fat and spices, they were ripened for 14 d. Then they were vacuum-packaged and stored for 80 d at 4℃. The effects of grape seed flour (GSF; 0%, 0.75%, 1.5%, 3%) on the physical-chemical properties (pH, moisture, fat, protein, free fatty acids, thiobarbituric acids, diameter reduction, ripening yield, instrumental colour), microbiological properties (total aerobic mesophilic and lactic acid bacteria, Enterobacteriaceae, mould and yeast) and sensory properties of the sausages were investigated. Grape seed flour decreased moisture, TBA, diameter reduction, instrumental colour (a, b) values and sensory analysis scores during the ripening period; it also decreased TBA, instrumental colour (L, a, b) values, total aerobic mesophilic and lactic acid bacteria counts during the storage period. It was concluded that grape seed flour has a potential application as an additive in dry fermented sausages.

• BMB Reports
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• v.31 no.2
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• pp.196-200
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• 1998

Zeins, maize storage proteins, are retained in the endoplasmic reticulum (ER) during the subcellular targeting process without the ER retention signal. Circumstantial data indicate that the 27K zein is an ER transmembrane protein. The potential transmembrane domain may permit the 27K zein to remain in the ER. This study investigated the potential transmembrane feature by employing alkaline extraction, proteinase K digestion, and surface biotinylation on isolated intact protein bodies. These assays consistently support the possibility of the 27K zein as a transmembrane protein. The 27K zein polypeptide was shown to be associated with alkali-stripped membranes. The polypeptide was digested by proteinase K to a smaller fragment. According to surface biotinylation, the 27K zeins was labeled to the exclusion of other classes of zeins. This study, therefore, concludes that the 27K zein has an ER transmembrane domain, which may serve as an anchor for zeins' ER retention.

• Applied Microscopy
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• v.21 no.2
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• pp.117-125
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• 1991

This study has been carried out to investigate the development of dictyosome, and roles of dictyosome about the formation of spherosome in the endosperm cell during seed formation of Panax ginseng with electron microscope. The result is as follows; In the endosperm cells of early stage during seed formation of Panax ginseng, plastid, mitochondria, endoplasmic reticulum, dictyosome and ribosomes are evenly distributed in cytoplasm. Electron lucent vesicles derived from dictyosome are observed in endosperm cells. Vesicles that contain low electron density are derived from forming face of dictyosome and releases into the cytosol. This vesicles formed multi vesicular body or fused with the plasma membrane. The spherical spherosomes are formed from dictyosome containing the lipid materials of even electron density and are gradually increased in size and number. Dictyosome is located in between vacuole and spherosome and it's cisternae form a semicircle and a circle. Some membrane of the protein body that accumulate the storage protein are originate from the spherical vacuole which interfused between vesicles and vacuoles derived from dictyosome.

• Preventive Nutrition and Food Science
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• v.13 no.4
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• pp.370-374
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• 2008

The Gelidium corneum (GC)-whey protein isolate (WPI) blend film containing grapefruit seed extract (GSE) was prepared by incorporating different amounts (0, 0.02, 0.04, 0.08, 0.1%) of GSE into the film. The film's tensile strength (TS) and water vapor permeability (WVP) were improved by the addition of GSE. The film containing 0.1% GSE had a TS of 3.27 MPa, whereas the control had 2.64 MPa. WVP of the film was also significantly decreased by the addition of GSE. Addition of 0.1% GSE decreased the populations of Escherichia coli O157:H7, Listeria monocytogenes, and Salmonella Typhimurium by 1.0, 1.6, and 0.6 log CFU/g, respectively, compared to the control. Fish paste was packed with the GC-WPI blend film containing GSE, and microbial change in the fish paste inoculated with E. coli O157:H7, L. monocytogenes, and S. Typhimurium during storage was examined. Populations of E. coli O157:H7, L. monocytogenes, and S. Typhimurium were decreased by 0.60, 0.48, and 0.85 log CFU/g, after 7 day of storage, respectively. These results suggest packaging fish paste in the GC-WPI blend film containing GSE can extend the shelf life.