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Physicochemical Studies of Caroubin: A Gluten-like Protein

2001; American Chemical Society; Volume: 49; Issue: 7 Linguagem: Inglês

10.1021/jf010076u

1520-5118

Yulan Wang, Peter Belton, Helene Bridon, Élisabeth Garanger, Nikolaus Wellner, Mary L. Parker, Alex Grant, Pierre Feillet, Tim R. Noel,

Fermentation and Sensory Analysis

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. Keywords: NMR; FTIR; electron microscopy; DSC; caroubin; gluten