Abstract
Due to the growing demand for human-edible protein sources, microalgae are recognized as an economically viable alternative source of proteins. The investigation into the structural characteristics and functional properties of microalgin is highly significant for its potential application in the food industry as an alternative source of protein. In this research, we extracted protein from Euglena gracilis by using alkaline extraction and acid precipitation and investigated its structural characteristics and functional properties in different acidic and alkaline environments. The molecular weight distribution of Euglena gracilis protein (EGP), as revealed by the size exclusion chromatography results, ranges from 152 to 5.7 kDa. EGP was found to be rich in hydrophobic amino acids and essential amino acids. Fourier infrared analysis revealed that EGP exhibited higher α-helix structure content and lower β-sheet structure content in alkaline environments compared with acidic ones. EGP exhibited higher foaming properties, emulsifying activity index, solubility, free sulfhydryl, and total sulfhydryl in pH environments far from its isoelectric point, and lower fluorescence intensity (2325 A.U.), lower surface hydrophobicity, larger average particle size (25.13 µm), higher emulsifying stability index, and water-holding capacity in pH environments near its isoelectric point. In addition, X-ray diffraction (XRD) patterns indicated that different acidic and alkaline environments lead to reductions in the crystal size and crystallinity of EGP. EGP exhibited high denaturation temperature (T(d); 99.32 °C) and high enthalpy (ΔH; 146.33 J/g) at pH 11.0, as shown by the differential scanning calorimetry (DSC) results. The findings from our studies on EGP in different acidic and alkaline environments provide a data basis for its potential commercial utilization as a food ingredient in products such as emulsions, gels, and foams.