4.7 Article

Physicochemical studies of caroubin: A gluten-like protein

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 49, Issue 7, Pages 3414-3419

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf010076u

Keywords

NMR; FTIR; electron microscopy; DSC; caroubin; gluten

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It has been reported that caroubin, a protein mixture obtained from carob seeds, has rheological properties similar to those of gluten. Comparative studies of the effects of hydration and temperature on caroubin and gluten were carried out with the aid of NMR, FTIR, scanning electron microscopy, and differential scanning calorimetry techniques. The results show that caroubin has a more ordered structure than gluten and that hydration has little effect on its secondary structure when compared to gluten. Caroubin is more easily accessible to water than gluten, suggesting that caroubin is more hydrophilic in nature. On hydration, caroubin, like gluten, forms fibrillar structures and sheets.

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