Specificity of a wheat gluten aspartic proteinase.

@article{Bleukx1998SpecificityOA,
  title={Specificity of a wheat gluten aspartic proteinase.},
  author={W Bleukx and Kristof Brijs and Sophie Torrekens and Fred van Leuven and Jan A Delcour},
  journal={Biochimica et biophysica acta},
  year={1998},
  volume={1387 1-2},
  pages={
          317-24
        }
}

• W Bleukx, Kristof Brijs, +2 authors Jan A Delcour
• Published 1998 in Biochimica et biophysica acta

The substrate and peptide bond specificities of a purified wheat gluten aspartic proteinase (GlAP) are studied. GlAP shows maximum gluten hydrolysing activity at pH 3.0. At this pH, especially the wheat high molecular weight glutenin subunits (HMW-GS) and to a lesser extent the low molecular weight glutenin subunits and gliadins are hydrolysed. GlAP has no obvious effect on albumins and globulins. In its action on oxidised insulin B-chain, GlAP forms eight peptides and has high specificity for… CONTINUE READING

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