Researchers of the Ministry of Agriculture, Forestry, and Fisheries of Japan have developed mutant soybean cultivars containing glycinin of limited subunit compositions, such as only group I, only group II, and only A5A4B3, in addition to only A3B4 (22,23). In collaboration with them, we prepared glycinin (group I, group II, A3B4, and A5A4B3) from these mutant cultivars and analyzed their structural features (unpublished data). On gel filtration chromatography, subunits having the longer hypervariable region eluted faster. In other words, A5A4B3 and group II eluted faster than A3B4 and group I did, respectively. These results indicate that the variable regions influence the dimensions of glycinin similarly to the extension region of P-conglycinin. The thermal stability of A3B4 (87.2°C) was slightly lower than those of the other subunits (92.9-95.0°C), but group II containing A3B4 exhibited thermal stability similar to the others. Therefore, the effect of subunit compositions on the thermal stability is not significant. The order of surface hydro-phobicity on a hydrophobic column chromatography was group I < 11S < A3B4 < group II < A5A4B3. Thus, the surface hydrophobicity of glycinin comprised of several subunits is the arithmetic mean of those of individual subunits. Further, we confirmed that the molecular surfaces of the three dimensional structures of recombinant proglycinin A1aB1b and native glycinin A3B4 corresponded to the difference of surface hydrophobicity on a hydrophobic column chromatography. However, it is difficult to discuss the difference of the thermal stability in detail, because we have only determined the three dimensional structure of A3B4 among native glycinins.
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