Gliadins polymerized with cysteine: effects on the physical and water barrier properties of derived films

Biomacromolecules
Pilar Hernandez-MunozRafael Gavara

Abstract

To study the effects of disulfide bonds on certain functional properties of films made from the wheat gluten proteins gliadin and glutenin, cysteine was used to promote the formation of interchain disulfide bridges between gliadins in 70% ethanolic solution. Disulfide-mediated polymerization of gliadins was confirmed by means of SDS-PAGE analysis. After chemical treatment of gliadins, films were solution cast and the effects of both glycerol (used as a plasticizer) and relative humidity were studied on water vapor permeability, moisture sorption isotherms at 23 degrees C, and the optical properties of the films. The results were compared with those obtained from analogous films made from untreated glutenin macromolecules. Cysteine-mediated polymerization of gliadins improved the water vapor resistance of films achieving values close to those obtained for glutenin films. Development of intra- and interchain disulfide bonds did not change the moisture sorption capacity of the films but transparency was slightly diminished.

References

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Oct 1, 1959·Archives of Biochemistry and Biophysics·R W JONESF R SENTI
Dec 11, 2003·Journal of Agricultural and Food Chemistry·Pilar Hernández-MuñozRafael Gavara

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Citations

May 24, 2011·Journal of Agricultural and Food Chemistry·M Pau BalaguerPilar Hernandez-Munoz
Sep 3, 2009·Journal of Food Science·Naoko Yuno-OhtaTomomi Kataoka
Jan 21, 2012·Journal of Food Science·Suresh NeethirajanShigeru Sugiyama
Feb 10, 2010·Biomacromolecules·Bert LagrainJan A Delcour

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