Distribution and in Vitro Availability of Selenium in Selenium-Containing Storage Protein from Selenium-Enriched Rice Utilizing Optimized Extraction

2010 ◽  
Vol 58 (17) ◽  
pp. 9731-9738 ◽  
Author(s):  
Yong Fang ◽  
Brittany Catron ◽  
Yaofang Zhang ◽  
Liyan Zhao ◽  
Joseph a. Caruso ◽  
...  
1999 ◽  
Vol 22 (2) ◽  
pp. 197-206 ◽  
Author(s):  
M. Abd El-Mohsen ◽  
K. Khaled ◽  
M. Fetouh ◽  
H. Ahmed

2002 ◽  
Vol 16 (2) ◽  
pp. 113-120 ◽  
Author(s):  
S.K. Yadav ◽  
S. Sehgal

Spinach ( Spinacia oleracia) and amaranth ( Amaranthus tricolor) leaves were stored in polyethylene bags and without packing for 24 and 48 hours in a refrigerator at 5°C and 30°C in polyethylene bags. The fresh leaves were also dried (oven and sun), blanched (5, 10 and 15 min) and cooked in an open pan and a pressure cooker. The processed leaves were analysed for total iron, its availability and antinutrient content. The iron content of these leaves varied from 26.54 to 34.14 mg/l00g, dry weight and its HCl-extractability and in vitro availability were 62.11–67.18% and 3.03–3.97% of total respectively. Drying and storage had no significant effect on total iron content, Hel-extractability and availability ( in vitro), while blanching and cooking resulted in significant improvement of iron availability, and a significant reduction in oxalic acid content, while only blanching significantly reduced phytic acid and polyphenol contents. Thus cooking and blanching are good ways to improve HCl-extractability and in vitro availability of iron.


Química Nova ◽  
2011 ◽  
Vol 34 (2) ◽  
pp. 186-189 ◽  
Author(s):  
Najma Sultana ◽  
Erum Humza ◽  
Muhammad Saeed Arayne ◽  
Urooj Haroon

Meat Science ◽  
1997 ◽  
Vol 45 (4) ◽  
pp. 473-483 ◽  
Author(s):  
Marina Santaella ◽  
Isabel Martínez ◽  
Gaspar Ros ◽  
MaJesús Periago

1995 ◽  
Vol 305 (1) ◽  
pp. 21-23 ◽  
Author(s):  
A Treffry ◽  
D Gelvan ◽  
A M Konijn ◽  
P M Harrison

Ferritin is an iron-storage protein ubiquitous in mammals, plants and bacteria. It can be reconstituted, in vitro, from the apoprotein and Fe(II) salts in the presence of dissolved oxygen. Recently it has been reported that caeruloplasmin can facilitate apoferritin reconstitution and that iron oxidized by caeruloplasmin is sequestered within the ferritin shell. Here we show that the primary effect of adding caeruloplasmin to horse spleen ferritin during reconstitution is the competition between the two molecules for the iron. This competition results in overall increased rates of iron oxidation and a mixture of products, namely iron-containing ferritin and iron hydroxy polymers attached to caeruloplasmin. Iron oxidized by caeruloplasmin is not incorporated, to any significant extent, into horse spleen ferritin.


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