Effect of Electron Microscopy Fixation pH on the Ultrastructure of Soybean Protein Bodies

2000 ◽  
Vol 48 (2) ◽  
pp. 302-304 ◽  
Author(s):  
W. L. Boatright ◽  
K. S. Kim
Keyword(s):  
Electron Microscopy ◽  
Soybean Protein ◽  
Protein Bodies

scholarly journals The influence of jasmonic acid on the amount and the distribution of cysteine proteinase PLCP-2 in healthy and PVYNTN infected potato plants (Solanum tuberosum L.)

2002 ◽  
Vol 38 (SI 1 - 6th Conf EFPP 2002) ◽  
pp. S95-S98
Author(s):  
M. Pompe-Novak ◽  
M. Tušek-Žnidarič ◽  
B. Štrukelj ◽  
M. Ravnikar
Keyword(s):  
Electron Microscopy ◽  
Solanum Tuberosum ◽  
Jasmonic Acid ◽  
Cell Walls ◽  
Cysteine Proteinase ◽  
Solanum Tuberosum L ◽  
Cell Types ◽  
Protein Bodies ◽  
Potato Plants

The localization of cysteine proteinase PLCP-2 was investigated in potato plants (Solanum tuberosum L.) cultivar Désirée by electron microscopy. Healthy and PVY<sup>NTN</sup> infected potato plants were grown in vitro on media with or without a supplement of jasmonic acid. We had already shown that PLCP-2 is present in leaves, stems, tips of shoots and tips of roots of healthy and PVY<sup>NTN</sup> infected plants. It was detected in various cell types in protein bodies in vacuoles, in cytoplasm and in cell walls. There were significantly larger amounts of PLCP-2 in plants grown on medium with a supplement of jasmonic acid in both healthy and virus infected plants. More protein bodies in vacuoles were found in plants grown on medium with addition of jasmonic acid.

Structural changes in whole milk during the production of sterile concentrates: an electron microscope study

1970 ◽  
Vol 37 (3) ◽  
pp. 513-522 ◽  
Author(s):  
P. W. Board ◽  
Joan M. Bain ◽  
D. W. Gove ◽  
J. T. Mullett
Keyword(s):  
Electron Microscopy ◽  
Structural Changes ◽  
Physical Stability ◽  
Protein Bodies ◽  
Large Protein ◽  
Casein Micelles ◽  
Fat Globules ◽  
Whole Milk ◽  
Freeze Dried ◽  
Average Size

SummaryElectron microscopy was used to study the effect of addition of NaOH, forewarming, homogenization, concentration, and heat sterilization on the structure of whole milk during the production of 4 heat-sterilized concentrates that showed different degrees of physical stability. The samples were prepared for electron microscopy by adding fixative either to liquid or freeze-dried material, and then embedding for sectioning.Noticeable structural changes occurred during forewarming of samples containing added NaOH, during homogenization, and during heat sterilization. Addition of NaOH and forewarming decreased the closeness of packing of the subunits in the casein micelles. Homogenization reduced the average size of the fat globules, and protein became attached to their surfaces. Heat sterilization caused coalescence of protein. In non-homogenized sterilized concentrate with added NaOH, protein bodies of about 100 times the volume of the original casein micelles were formed; these were free-floating and the concentrate was stable. In non-homogenized sterilized concentrate with no added NaOH the protein bodies were about 15 times the size of the casein micelles and bridged to each other, thereby forming a sediment consisting of large irregular particles. Very large protein bodies containing fat globules formed during heat sterilization of the homogenized samples, both in the presence and in the absence of NaOH, and were responsible for the formation of sediment in these 2 products.Needle crystals observed in most samples were identifed as CaCO3. H2O by selected area diffraction; KC1 crystals were also detected.

The Analysis on Composition and Structure of the Eri-Silk

2013 ◽  
Vol 423-426 ◽  
pp. 386-390 ◽  
Author(s):  
Wen Zhong Wang ◽  
Lei Zhao ◽  
Li Shan Fan
Keyword(s):  
Electron Microscopy ◽  
Silk Fibroin ◽  
Soybean Protein ◽  
Main Structure ◽  
Composition And Structure ◽  
Protein Fiber ◽  
Infrared Spectral ◽  
Folding Structure ◽  
Α Helix ◽  
Eri Silk

The eri-silk was degummed by Alkaline protease,the chemical composition of the eri-silk was analyzed and the internal structure of the retting eri-silk was analyzed by infrared spectral, also the vertical form of the was tested by electron microscopy and using thermal analysis to study the thermal properties of the eri-silk. The results showed that the highest content in the eri-silk was alanine, followed by acetic acid; The heat resistance of the eri-silk was worse than the soybean protein fiber and wool, the the surface of the degumming eri-silk was smooth, there was obvious dents between two silk fibroin; the structure of the eri-silk fibroin contain α-helix and β-folding structure which is the most main structure, there is distinguishing peak characteristics of AmideI at wave 1661.

scholarly journals A WOOD BIOPLASTIC COMPOSITE FROM SOY FLOUR AND SAWDUST

2020 ◽  
Vol 50 (2) ◽  
pp. 95-100
Author(s):  
Natalia Edith Suarez ◽  
María Cristina Inalbon ◽  
Camilo Ignacio Meyer ◽  
Silvina Andrea Regenhardt ◽  
Hernán Antonio Duarte ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Soybean Protein ◽  
Soy Flour ◽  
Lignocellulosic Material ◽  
Processing Conditions ◽  
Wood Sawdust ◽  
Plastic Composite ◽  
Test Pieces ◽  
Hardness Tests ◽  
Scanning Electron

The influence of the processing conditions and composition on the properties of biocomposites made of a bioplastic matrix from soybean protein, crosslinked with glutaraldehyde, reinforced with lignocellulosic material from wood sawdust (Wood Bio-Plastic Composite, WBPC) was investigated. The WBPCs were obtained by thermocompression applying a pressure of 70 bar at 100 and 120 °C for 30 or 60 minutes. Several test pieces were prepared varying the crosslinker/protein and protein/sawdust ratios. The samples obtained were characterized by scanning electron microscopy (SEM), flexural and hardness tests, and water absorption and swelling, according to international ASTM standards. The crosslinking of the protein improves the mechanical properties of the biocomposites, especially when contents of bioplastic matrix and crosslinker are low. It was also verified that the WBPCs prepared in this work recover their original shape and dimensions after immersion in water and subsequent drying. The results were explained considering crosslinker-protein and protein-sawdust interactions.

Occurrence of Globoid Crystals in Cotyledonary Protein Bodies of Pisum sativum as Influenced by Experimentally Induced Changes in Mg, Ca and K Contents of Seeds

1985 ◽  
Vol 12 (4) ◽  
pp. 341 ◽  
Author(s):  
JNA Lott ◽  
PJ Randall ◽  
DJ Goodchild ◽  
S Craig
Keyword(s):  
Electron Microscopy ◽  
Pisum Sativum ◽  
Energy Dispersive ◽  
Protein Bodies ◽  
Rare Occurrence ◽  
Review Of Literature ◽  
X Ray ◽  
K Concentration ◽  
Induced Changes ◽  
Experimentally Induced

In many species globoid crystals in protein bodies of seeds are very common while in other species they are rarely observed. A review of literature suggested that the balance between divalent (Mg2+ and Ca2+) and monovalent (K+) cations may be important in determining whether or not globoid crystals will form. To test this hypothesis, experiments were carried out to add Mg and Ca, or Ca alone, to pods developing on K-deficient pea plants. While it was possible to cause a reduction in K concentration and increases in Mg and Ca concentrations, any changes to the normal mineral storage pattern in pea cotyledons were remarkably small. In some treatments, statistically significant increases in the ratio (Mg + Ca)/K were obtained and the sample with the greatest increase was examined in detail by electron microscopy and energy dispersive X-ray analysis. In this sample globoid crystals were common, in contrast to their normally rare occurrence in pea cotyledonary tissue.

Microstructure and Hydrodynamic Properties of Soybean Protein Bodies in Solutions

1983 ◽  
Vol 48 (3) ◽  
pp. 695-702 ◽  
Author(s):  
CHERL-HO LEE ◽  
CHAN-SHICK KIM ◽  
HAN-CHUL YANG
Keyword(s):  
Soybean Protein ◽  
Protein Bodies ◽  
Hydrodynamic Properties
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