Abstract
The associative phase behavior of cricket protein isolate (CPI) and sodium alginate (AL) in aqueous solutions was explored using turbidimetry, methylene blue spectroscopy, zeta potentiometry, dynamic light scattering, and confocal microscopy as a function of pH, biopolymer ratio, total biopolymer concentration (CT), and ionic strength. When both biopolymers had net-negative charges, soluble complexes formed between pH 6.0 and 8.0, however when both biopolymers had opposing net charges, insoluble complexes formed as complex coacervates below pH 5.5, defined as pHφ1, followed by precipitates below another critical pH 3.0 (pHp). Increasing the CPI:AL weight ratio or CT facilitated complex formation, and the addition of salts (NaCl/KCl) had a salt-enhancement and salt-reduction impact at low and high salt concentrations, respectively. Ionic interactions between oppositely charged CPI and AL were mainly responsible for the formation of their insoluble complexes, while hydrogen bonding and hydrophobic interactions also played significant roles.
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