PubMed · 4139615
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1974-11-16. Letter: Diet and multiple sclerosis.. https://pubmed.ncbi.nlm.nih.gov/4139615/
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The effect of temperature on gluten conditioned at the following water contents, 0%, 13%, and 47% (wet weight basis), was studied by FTIR spectroscopy over the temperature range of 25-85 degrees C. A detailed discussion of the assignment of the amide I band is given. At 0% hydration no changes in the secondary structure with temperature could be detected; spectra were consistent with a tight disordered structure with many protein-protein interactions. At 13% hydration, distinctive changes occurred in the low-frequency region of the amide I band (1,630-1,613 cm(-1)). This was attributed to changes in the beta-sheet structure. On cooling to 25 degrees C, these changes were mainly reversed. It was noted that most of the changes observed occurred above the glass transition temperature. At 47% hydration, more complex changes took place: as the temperature was raised distinct bands at 1,630 and 1,613 cm(-1) merged. However, this process was partially reversed, with recovery of both bands, on cooling. The significance of these results in relation to other changes in gluten proteins in flour and dough with temperature and water content is discussed.
The contribution of rice as a protein source is important. Rice seed protein can be divided into four forms, glutelin (57 kDa, 37-39 kDa, 22-23 kDa), prolamine (13 kDa), albumin (16 kDa) and globulin (10 kDa, 26 kDa) on its solubility. Glutelin is the major storage protein of rice and accounted for 80% of total protein found in the rice grain, the mature glutelin comprises an acidic (37-39 kDa) and an basic subunit (22-23 kDa) coming from a common precursor (57 kDa) by post-transcriptional hydrolytic cleavage. Prolamine is the second important. Rice seed proteins localize in two types of protein bodies, PB-I, PB-II. PB-I containing prolamine is indigestible, whereas PB-II being rich in glutelin is digestible. The nutritional value of rice could thus be raised by improving its digestible protein glutelin content. On the other hand, the character of low digestible protein is also an important target of rice breeding. Low protein rice is required for the diet of patients with kidney disease. Three glutelin mutants, W3660, W204, W379, were found by screening 168 rice varieties through SDS-PAGE analysis of the seeds total proteins. The amounts of 37-39 kDa and 22-23 kDa glutelin subunits were much lower and that of 13 kDa prolamine polypeptide was higher in W3660 seeds than in ordinary rice; The amounts of 37-39 kDa and 22-23 kDa glutelin subunits in W204 or W379 seeds were between those in W3660 and ordinary rice. Especially, in W379 seed, there was a large quantity of 57 kDa polypeptide. For characterizing the genetics of the glutelin mutant, the cross population between W3660 and Otorokimochi was constructed. SDS-PAGE analysis of the progeny seed total proteins showed, low glutelin content was always accompanied by high prolamine content; all F1 seeds had low glutelin and high prolamine content; the segregation of low glutelin and normal type in F2 seeds was 3:1; the genotypes of F2 plants were deduced by the analysis of F3 seeds, and among F2 plants the ratio of homozygotes of low glutelin, heterozygotes of low glutelin and homozygotes of normal type was about 1:2:1. These results proved that the trait of low glutelin and high prolamine was controlled by a single dominant gene and could be inherited by its progeny.
This work describes the application of (1)H magic angle spinning (MAS) nmr to the study of hydrated 1Dx5 wheat high-M(r) subunit. 1Dx5 is a water-insoluble 88 kDa protein, associated with good baking performance, and whose structure in the solid and low-hydration states is not known. High-resolution MAS (HR-MAS) results in a threefold resolution improvement of the (1)H spectra of the hydrated wheat protein, compared to standard MAS. The spectral resolution achieved enables, for the first time, two-dimensional nmr methods to be employed for the study of hydrated 1Dx5 and the assignment of the spectrum to be carried out on the basis of total correlated spectroscopy and (13)C/(1)H correlation experiments. Considerable shifts are observed for some resonances, relative to the chemical shifts of amino acids in solution, indicating that specific interactions occur in the hydrated protein network. Two main environments are identified for glutamine residues, Q(1) and Q(2), and these were characterized in terms of possible conformation and relative dynamics, with the basis of comparison between the single 90 degrees spectrum and the Carr-Purcel-Heiboom-Gill (CPMG) spectrum. The Q(1) residues are proposed to be situated in protein segments that adopt the beta-sheet conformation and that remain relatively hindered, possibly by hydrogen bonds involving the glutamine amide groups. On the other hand, Q(2) residues are proposed to be situated in a more mobile environment, adopting a looser conformation, possibly a beta-turn conformation. Based on the proximity of the Q(2) residues with glycine residues, as viewed by the nuclear Overhauser effect spectroscopy experiment, it is proposed that the protein segments that form the more mobile (or loop) sections of the network are rich in both glutamine and glycine residues.