Modulating the textural characteristics of whey protein nanofibril gels with different concentrations of calcium chloride.

Protein nanofibrils with 10-20 nm diameters were formed by heating whey protein solution at pH 2.0. Nanofibrils solution was deacidified slowly through dialysis followed by adding different amounts of CaCl2 (0-80 mM) into the dialysis water resulting in formation of a soft viscoelastic gel over time. The gel fabricated from the nanofibrils solution dialyzed against distilled water with 0 mM CaCl2 had zero ash content. Fourier transform infra-red spectroscopy revealed a change in the pattern of hydrogen bond formation in gel network by calcium chloride. The higher the ash content of gels, the lower was the storage modulus and fracture stress of samples. Gels with higher ash contents had a more porous microstructure which was attributed to the diminished hydrophobic interactions and hydrogen bonding among nanofibrils by the action of chloride. Higher ash contents also led to higher water holding capacity of gels which was attributed to the influence of the strongly hydrated calcium ions that interacted with the non-charged regions of proteins via site-specific interactions.

Comparative study on composition and functional properties of brewer's spent grain proteins precipitated by citric acid and hydrochloric acid.

Brewer's spent grain (BSG) is an abundant agro-industrial residue and a sustainable low-cost source for extracting proteins. The composition and functionality of BSG protein concentrates are affected by extraction conditions. This study examined the use of citric acid (CA) and HCl to precipitate BSG proteins. The resultant protein concentrates were compared in terms of their composition and functional properties. The BSG protein concentrate precipitated by CA had 10% lower protein content, 5.8% higher carbohydrate, and 5.4% higher lipid content than the sample precipitated by HCl. Hydrophilic/hydrophobic protein and saturated/unsaturated fatty acid ratios increased by 16.9% and 26.5% respectively, in the sample precipitated by CA. The formation of CA-cross-linkages was verified using shotgun proteomics and Fourier transform infrared spectroscopy. Precipitation by CA adversely affected protein solubility and emulsifying properties, while improving foaming properties. This study provides insights into the role of precipitants in modulating the properties of protein concentrates.