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The influence of genotypic variation in protein composition on emulsifying properties of soy proteins
Author(s) -
Pesic Mirjana B.,
VucelicRadovic Biljana V.,
Barac Miroljub B.,
Stanojevic Sladjana P.
Publication year - 2005
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-005-1126-x
Subject(s) - soy protein , emulsion , chemistry , storage protein , composition (language) , monomer , food science , plant protein , protein isolate , positive correlation , biochemistry , gene , polymer , organic chemistry , medicine , linguistics , philosophy
This study describes the relationship between the emulsifying properties of soybean proteins and their composition, i.e., glycinin (11S) and β‐conglycinin (7S). Twelve investigated soybean genotypes showed significant differences in storage protein composition. The β‐conglycinin concentration positively correlated with extractable soluble protein content, which was positively correlated with protein extractability. These data suggest that the level of β‐conglycinin has a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the 11S∶7S ratio and strongly and negatively correlated with the concentration of β‐conglycinin. The emulsion stability index (ESI) showed a moderate positive correlation with the monomeric form of glycinin and a strong positive correlation with the ratio of the monomeric to dimeric form of glycinin. No association was evident between ESI and EAI. Also, no relationship was found between ESI or EAI and extractability. Based on these data, it appears that the 11S∶7S ratio strongly reflects the ability of soybean proteins to form emulsions, whereas the ratio of the two different forms of glycinin may be crucial factors for the stability of soybean protein emulsions. Thus, understanding the relationship between protein composition and functionality could be useful for further improvement of functional behavior of soy proteins in food systems.