Disulphide bonds in wheat gluten: cystine peptides derived from gluten proteins following peptic and thermolytic digestion.

@article{Keck1995DisulphideBI,
  title={Disulphide bonds in wheat gluten: cystine peptides derived from gluten proteins following peptic and thermolytic digestion.},
  author={Bettina Keck and Peter Koehler and Herbert Wieser},
  journal={Zeitschrift fur Lebensmittel-Untersuchung und -Forschung},
  year={1995},
  volume={200 6},
  pages={432-9}
}
Gluten from the wheat variety Rektor was extracted with 70% aqueous ethanol. The insoluble portion (whole glutenin) was partially hydrolysed with trypsin at pH 6.5 and separated on a Sephadex G25 column. The high molecular weight fraction 1 was further hydrolysed with pepsin at pH 2.0. To remove low molecular weight proteins, a portion of whole glutenin was extracted with dilute acetic acid. The residue (enriched glutenin), which contained mostly LMW and HMW subunits of glutenin, was hydrolysed… CONTINUE READING

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