In order to assess the potential of fractionated Schizochytrium sp. protein as functional proteins, the proteins were fractionally extracted. The structure, thermal characteristic and cross-linking interaction of proteins, along with the gel properties of heat-induced gels were analyzed and compared to those of albumin from chicken egg white (ACEW). Water fraction of Schizochytrium sp. protein (WFSP) was identified as the dominant fractionated protein. Classified as globular proteins, WFSP exhibited a molecular weight range of 30-250 kDa. Compared to ACEW, WFSP displayed a significantly lower denaturation temperature, indicating reduced energy consumption during food processing. Moreover, at a concentration of 50 g/L, WFSP gels displayed superior strength and stability by higher G' (114.7 kPa) and fracture strain (2.38 %) compared to ACEW gels (92.2 kPa and 1.33 %). Besides, WFSP gels had lower hardness, chewiness and water holding capacity, but higher springiness and cohesiveness than ACEW gels. WFSP formed porous particulate stranded three-dimensional gel network structures with uniform pore size, flat surface and complete sheet. The temperature sweeps and protein-protein interactions results suggested that hydrogen bonds played a dominant role in the formation of WFSP gel network. Overall, WFSP exhibits excellent gelation properties and holds promise as a functional protein for food production.
Keywords: Fractionation; Gelation property; Microalgae; Protein.
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