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ARS Home » Southeast Area » Raleigh, North Carolina » Soybean and Nitrogen Fixation Research » Research » Publications at this Location » Publication #159195
Title: GELLING MECHANISMS OF COMMERCIALLY PREPARED SOY PROTEIN ISOLATES

Author
item Kwanyuen, Prachuab
item MCKLEM, L - NC STATE UNIV
item LUCK, P - NC STATE UNIV
item LANIER, T - NC STATE UNIV
item Wilson, Richard

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: 1/20/2003
Publication Date: 5/4/2003
Citation: Kwanyuen, P., Mcklem, L.C., Luck, P.J., Lanier, T.C., Wilson, R.F. 2003. Gelling mechanisms of commercially prepared soy protein isolates [Abstract]. Annual Meeting and Expo of the American Oil Chemists' Society, p. 113.

Interpretive Summary:

Technical Abstract: Gelling mechanism of commercially prepared soy protein isolates is quite different from isolates prepared in laboratory. Using thermal reversibility with frequency sweep monitoring and chemical modifiers, on isolates commercially prepared from two soybean varieties with different in their amino acid and protein compositions, has revealed the molecular forces involve in the gelation of these isolates. Soy protein isolates gelled upon hydration and were strengthened by thermal treatment indicated by an increase in the final gel strength while holding at the end point temperature. However, additional thermal treatment did not enhance gelling properties of the isolates. Frequency sweep plots showed that combination of hydrogen bonding and hydrophobic interactions were primarily contributing to gelation of the isolates. Hydrogen bonds were involved in initial gel formation and increase in gel rigidity during cooling while hydrophobic interactions increased gel rigidity during holding the temperature at end point. Disulfide bonds also contributed in initial gel structure and stabilization but were not essential for gelation. Differences in gelling behavior of the isolates commercially prepared from the two soybeans were possibly due to processing variations and/or their protein composition.