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Cereal Chem 72:176-181  |  VIEW ARTICLE

Cathodic Peroxidases of Durum Wheat Flour.

R. Iori, B. Cavalieri, and S. Palmieri. Copyright 1995 by the American Association of Cereal Chemists, Inc. 

Two cathodic peroxidases (C1, C2) were purified from durum wheat (Triticum durum) flour by ion exchange chromatography. Both peroxidases appear to be homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis and isoelectric focusing. The isolated isoenzymes, both with a purity index (RZ) (A402nm/A280nm) of 3.7, are polypeptides of 39.7 kDa (C1) and 38.6 kDa (C2) and show pI above 9.3. The calcium ion strongly activates the C1 and C2 isoenzymes, which increases their specific activity 92 and 690 times, respectively, when stored at pH 6.5. This effect is presumably due to the stabilization of the heme-moiety structure, which was observed with the increase of the Soret band absorption. We consider this enzyme activity of great importance both in the production technology of high- quality pasta and more generally other bakery products.

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