Abstract

ε-Polylysine (EPL) is a food-grade antimicrobial peptide that forms complexes with proteins. Such complexes are potential carriers for targeted delivery of agents. To elucidate the formation of such complexes, the pH-induced phase transition of EPL and sodium caseinate (SC) complexes were characterized in terms of ionic strengths (I) and EPL/SC weight ratios (r). Electrostatic nanocomplexes (e.g. r = 2−3, I = 2 mM) were formed near the isoelectric point of SC using turbidimetry, dynamic light scattering, and ζ-potential measurements. Phase analyses revealed that the formation of nanocomplexes primarily depends on the I, and saturated binding was recorded above r = 2−2. Electrostatic potential modelling of EPL was employed to describe the interaction affinity. A three-dimensional phase boundary curve was established which divided the complexation into a nano-scale and phase separation. Atomic force microscopy images confirmed that nanocomplexes were spherical particles with uniform shapes. Morphologic examination using optical and scanning electron microscopy and Fourier transform infrared spectroscopy revealed that the nanocomplexes formed “sponge-like” precipitates at larger length scales. This work reveals the possible mechanism that drives the complexation of sodium caseinate and ε-Poly-l-lysine. This is expected to guide the construction of tailor-made protein complexes in industrial applications.

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