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Structure, trypsin inhibitor activity and functional properties of germinated soybean protein isolate
Author(s) -
Aijie Liu,
Shouwei Yin,
Li Li
Publication year - 2014
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.12386
Subject(s) - germination , hypocotyl , trypsin , trypsin inhibitor , in vitro , chemistry , soy protein , biochemistry , food science , enzyme , botany , biology
Summary The objective of this research was to investigate the effects of germination on functional and conformational properties as well as the in vitro trypsin digestibility of soy protein isolate ( SPI ). The influences of germination on the molecular properties of SPI were also evaluated. The germination degraded lipoxygenase, α, α' subunits of β‐conglycinin (7S) and acidic chains of glycinin (11S) of soybean. Concomitantly, the loss of tertiary structures of SPI occurred due to the germination. The trypsin inhibitor activity of germinated SPI presented a decreasing trend, followed by an increase in the growth of hypocotyls. The in vitro trypsin digestibility of germinated SPI followed a consistent trend with the trypsin inhibitor activity. The protein solubility ( PS ) and emulsifying properties of SPI were improved by the germination, in a hypocotyl length‐dependent manner. The data suggest that some selected functional properties and the in vitro digestibility of soy proteins can be improved by means of the germination.