Besides providing dietary fiber, wheat bran is a recognized source of protein and is considered a very valuable substitute for other protein-rich sources in the food and feed industry. Nonetheless, several factors affect protein bioavailability, including bran's layered structure. This study showed the influence on the release and protein modification of wheat bran of different bioprocessing methods involving the activation of endogenous enzymes of bran, the addition of an enzyme mixture having carbohydrase activity, and microbial fermentation. Bioprocessing in acidic conditions significantly enhanced the solubilization of protein from wheat bran, reaching the highest value in the treatment where the sole endogenous protease activity was activated. Bioprocessing through controlled fermentation allowed a more intense proteolysis and strongly impacted the in vitro digestibility of proteins. The combined use of starter cultures and cell-wall-degrading enzymes was characterized by the highest increase of phytase activity and total phenols.

Cereal Chem. 93(2):162-171Wheat bran contains good quality protein, but given its location inside aleurone cells, this protein has restricted digestibility. The aim of this work was to liberate and solubilize wheat bran proteins via cell wall degradation by using carbohydrate-hydrolyzing and proteolytic enzymes without causing extensive protein hydrolysis. Bran incubated with water (without added enzymes) for 16 h increased the solubilized organic nitrogen content from 14.0 to 42.8%. Enzymes with solely carbohydratehydrolyzing activity increased the water-soluble pentosan and reducing sugar contents but did not significantly increase protein solubilization or protein release from the aleurone cells. Enzymes with proteolytic activity significantly increased the solubilization of protein to 58.2% already at 4 h. Significant protein hydrolysis was detected with a high dosage of protease. However, based on light microscopy, the enzymatic treatment mainly modified the proteins in the subaleurone layer, and it was less effective on proteins inside the aleurone cells. With optimized protease treatment (3 h, 35°C, and 550 nkat/g), effective protein solubilization (>48%) without extensive protein hydrolysis (free amino nitrogen content <45 mg/L) was achieved. In conclusion, intensive solubilization of proteins in the subaleurone layer of wheat bran is possible by using exogenous enzymes with proteolytic activities. † Corresponding

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