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ARS Home » Southeast Area » Raleigh, North Carolina » Soybean and Nitrogen Fixation Research » Research » Publications at this Location » Publication #222434
Title: The Effect of Transglutaminase Crosslinking Reactions on Soy Protein vs. Heated Soy Protein Dispersions

Author
item CLARE, DEBRA - N.C. STATE UNIVERSITY
item HWANG, HYEMEE - N.C. STATE UNIVERSITY
item Kwanyuen, Prachuab
item DAUBERT, CHRIS - N.C. STATE UNIVERSITY

Submitted to: American Oil Chemists' Society Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 3/15/2008
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Previously, we created a thermally modified soy protein ingredient (mSPI) that was readily reconstituted in water and demonstrated improved heat stability and cold-set gel functionality compared to unheated SPI. Herein, we examined the effect of enzyme modification (microbial transglutaminase; mTGase) on equivalently prepared SPI and mSPI protein dispersions with respect to: (1) solubility, (2) the effects of temperature on polymerization reactions, (3) degree of cross-linking, (4) SDS-PAGE protein banding patterns before and after mTGase treatment, and (5) resultant altered functional parameters, such as apparent viscosity, after enzyme processing. Aggregate formation occurred in mSPI solutions which diminished solubility and heat stability. Notably, the mSPI substrate was not cross-linked to the same extent as SPI at either 37 degree C or 60 degree C. Perhaps, this was due in part to aggregate formation that limited accessibility to the TGase catalytic site. SPI and mSPI dispersions exhibited a yield stress and non-Newtonian flow behavior. In contrast, both enzyme treated samples demonstrated shear thinning properties. The apparent viscosity was significantly higher in TGase-treated SPI vs. Tgase treated-mSPI dispersions, both of which were greatly enhanced compared to non-enzyme control solutions. These differences in functionality will impact the design for future applications.