Literature DB >> 15244471

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

Pilar Hernández-Muñoz1, José M Lagarón, Amparo López-Rubio, Rafael 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.

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Year:  2004        PMID: 15244471     DOI: 10.1021/bm0499381

Source DB:  PubMed          Journal:  Biomacromolecules        ISSN: 1525-7797            Impact factor:   6.988


  1 in total

1.  Mechanistic investigation of capability of enzymatically synthesized polycysteine to cross-link proteins.

Authors:  Asako Narai-Kanayama; Tomoko Hanaishi; Keiichi Aso
Journal:  Biochem Biophys Rep       Date:  2016-07-21
  1 in total

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