Comparative Analysis of the Structural and Physicochemical Properties of Different Proteins in Lotus Seeds
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Abstract:
Lotus seed protein isolates and lotus seed fractionated proteins (albumin, globulin, prolamin, glutenin) were extracted, and the solubility, emulsification, molecular properties, and structural properties were compared. The results showed that protein in lotus seeds accounts for about 16.14% of the total dry weight, and the proportion of four graded proteins was about 55:6:0.1:25. Respectively, compared with the five different lotus seed proteins, The solubility of albumin was the highest, the Zeta potential had the lowest value of -21.3 mV, the particle size had the minimum value of 75.47 μm, and the emulsification of the isolated protein was the best. The isoelectric points of five different proteins were all around 4.9. Spectroscopic studies have shown that gliadin and glutenin fluoresce more strongly, the content of albumin and globulin α-helix was lower, while the content of gliadin and glutenin β-turn was higher. These results also indicate that the molecular flexibility of albumin and globulin is higher, which is closely related to solubility, ability to emulsify, and hydrophobicity. The experiments revealed the active structural relationship between the physicochemical properties and molecular structure of lotus seed protein isolates and fractionated proteins. This provides a theoretical basis for the further study of the functional properties of lotus seed protein.
