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Original Articles

Gelling Properties of Soybean β-Conglycinin Having Different Subunit Compositions

, , , , , & show all
Pages 1091-1096 | Received 03 Dec 2003, Accepted 27 Jan 2004, Published online: 22 May 2014
 

Abstract

The effects of protein concentration, and heating temperature and time on the gelling properties of soybean β-conglycinin (7S globulins) lacking the α or α′ subunit were compared with those of 7S containing all three subunits (α, α′, and β) to determine whether each subunit contributes equally. In most of the conditions, the relative order of gel hardness was α′-lacking > 7S > α-lacking. From Fourier transform infrared studies, the secondary structure change after heating was very similar among the three samples; thus, the secondary structural change is not the reason for the differences in gel hardness. By using scanning electron microscopy, we observed differences in strand thickness and the density of the gel network among the three samples. These differences correlated well with the differences in gel hardness.

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