Viscoelastic behavior, gelation properties and structural characterization of Deccan hemp seed (Hibiscus cannabinus) protein: Influence of protein and ionic concentrations, pH, and temperature.

This study investigates the viscoelastic behavior, gelling properties, and structural characteristics of Deccan hemp seed protein (DHSP) to overcome limitations in its application in food formulations. Small amplitude oscillatory shear measurements were employed to investigate the impact of protein concentration, pH, ionic concentration, and temperature on DHSP's rheological features. The study revealed that the 20 % protein dispersion had the highest storage modulus (G') and yield stress at 63.96 ± 0.23 Pa and 0.61 Pa, respectively. DHSP dispersion exhibited pseudo-plastic behavior across various conditions. The gelling performance was higher at pH 4 and 8 and at ionic concentration in the range of 0.1 M - 0.5 M. Gelation time and temperature were observed from the temperature ramp test. Structural characterizations, including fluorescence spectroscopy, circular dichroism spectra, FTIR spectra, SEM, AFM images, zeta potential analysis, and DSC, provided insights into DHSP's tertiary and secondary conformation, surface characteristics, and thermal properties. Notably, the study highlighted DHSP's exceptional rheological properties, making it a promising gelling material for the food and nutraceutical industries. The findings also offer new insights into DHSP's structural characteristics, suggesting potential applications in food packaging and product development within the food industry. [Display omitted] • Protein concentration, pH and ionic strength affected viscoelastic behavior of Deccan hemp seed protein (DHSP). • DHSP dispersion exhibited pseudo plastic-behavior for all the three factors. • Protein denaturation and aggregation influenced the temperature induced gelation. • The gelling property of the protein dispersion was higher at pH 4 and pH 8. • Fluorescence spectroscopy and circular dichroism confirmed tertiary and secondary structures of DHSP. [ABSTRACT FROM AUTHOR]