2009
DOI: 10.3923/ajb.2009.88.98
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Extraction, Characterization and Nutritional Properties of Two Varieties of Defatted Foxtail Millet Flour (Setaria italica L.) grown in China

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Cited by 18 publications
(20 citation statements)
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“…In this case, the protein bands in prolamin and glutelin were almost invisible. As described by Medici et al (2018), the molecular mass of the prolamin fraction was estimated at 22 kDa, while the molecular mass of glutelin extracted from two varieties of foxtail millet (white and yellow) was difficult to determine, as the SDS-PAGE image revealed many bands along the gel (Kamara, Ming, & Kexue, 2009). This is consistent with the results presented in this study.…”
Section: Discussionsupporting
confidence: 90%
“…In this case, the protein bands in prolamin and glutelin were almost invisible. As described by Medici et al (2018), the molecular mass of the prolamin fraction was estimated at 22 kDa, while the molecular mass of glutelin extracted from two varieties of foxtail millet (white and yellow) was difficult to determine, as the SDS-PAGE image revealed many bands along the gel (Kamara, Ming, & Kexue, 2009). This is consistent with the results presented in this study.…”
Section: Discussionsupporting
confidence: 90%
“…Lysine and iron percentage was higher noticed in all the tested crops but iron % was noticed least in E. coracana in comparison to wheat and rice (Table 2). Millets contain higher quantity of essential amino acids methionine and cytosine and are higher in fat content than maize, rice and sorghum (Kamara et al, 2009). The iron content of E. frumentacea was found higher 18.6±1.78 mg/100gm which is followed 3.9 in E. coracana.…”
Section: Resultsmentioning
confidence: 85%
“…These interactions depend on the type and nature of different amino acid residues on protein surfaces or cavities and the size of the cavity (Santos-Buelga & Scalbert, 2000;Bandyopadhyay et al, 2012). Foxtail millet flour is rich of diverse proteins (Kamara et al, 2009;Mohamed et al, 2009;Verma et al, 2015). We hypothesise that FMF proteins form complexes with blueberry polyphenols and anthocyanins through the interactions mediated by amino acids that possess an open conformation allowing hydrophobic interactions, hydrogen bonds between phenolic hydroxyl groups and carbonyl groups of peptide bonds (Hagerman & Butler, 1981;Hagerman et al, 1998).…”
Section: Discussionmentioning
confidence: 99%