Characterization of Heat-Set Gels from RuBisCO in Comparison to Those from Other Proteins

• Published in: Journal of agricultural and food chemistry Vol. 62; no. 44; pp. 10783 - 10791
• Main Authors: Martin, Anneke H, Nieuwland, Maaike, Jong, Govardus A. H. de
• Format: Journal Article
• Language: English
• Published: American Chemical Society, Books and Journals Division 2015
• Subjects: animals; deformation; denaturation; egg albumen; gel strength; gelation; gels; hydrogen bonding; hydrophobicity; ingredients; microstructure; protein sources; ribulose-bisphosphate carboxylase; spinach; temperature; whey protein
• ISSN: 0021-8561; 1520-5118

To anticipate a future shortage in functional proteins, it is important to study the functionality of new alternative protein sources. Native RuBisCO was extracted from spinach, and its gelation behavior was compared to other native proteins from animal and plant origins. Protein gels were analyzed for their mechanical gel properties during small and large deformation and for their microstructure. Heat-induced aggregation and network formation of RuBisCO resulted in gels with unique characteristics compared to, for example, whey protein and egg white protein. Having a very low critical gelling concentration and low denaturation temperature, RuBisCO readily forms a network with a very high gel strength (G′, fracture stress), but upon deformation it has a brittle character (low critical strain, low fracture strain). This breakdown behavior can be explained by the dominant role of hydrophobic and hydrogen bonds between RuBisCO molecules during network formation and by the coarse microstructure. RuBisCO was shown to exhibit high potential as a functional ingredient giving opportunities for the design of new textures at low protein concentration.