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By Neason A Eskin

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None of the fractions are, however, homogeneous. The 2S and 15S fractions are made up mainly of enzyme inhibitors and allergenic factors (Vaidehi and Kadam, 1989). The 7S globulins make up the bulk of the 7S fraction, while 11S globulin is the only protein in the 11S fraction. , 2006). g. , 2008). 3. Protein Structure and Properties The 7S and 11S globulins, because they make up the bulk of legume seed proteins, have been extensively studied. These globulins may be structurally similar, but differences exist from one legume to another in their subunit profiles and amino acid sequences, that give rise to differences in overall protein functionality.

The main effect of heating appears to be related to the translocation of moisture brought about by the temperature gradients in the grain. B. Prolonged Storage of Grains and Flour Pixton et al. 5 C) and low oxygen concentrations (< 2% by volume). 6%, were placed in bins in 1-ton lots. The moisture content did not change significantly over this period. The crude protein and salt-soluble protein content remained unchanged for both wheats irrespective of the storage conditions. 5% was observed for both wheat varieties, which was attributed to carbohydrate metabolism during the long storage period.

Studies by Raynes and Briggs (1985) showed increased a-amylase production in decorticated barley grains germinated with or without gibberellic acid. 9, indicate that the onset and amount of enzyme activity were affected by GA3 and K2SO4. The presence of K2SO4 appeared to delay the destruction of a-amylase (Briggs, 1968). , 1984). , 1981; Sargeant, 1979, 1980). This differed from a-amylase production in pre-mature excised embryo/scutellar tissue, where a-AMY2 was the predominant isoenzyme formed even in the presence of GA3.

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