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Abbasporrad, A.

Publications and source records attributed to Abbasporrad, A..

2 recordsLinked to original sources

Iron-mediated assembly of lactoferrin-alginate composites for iron encapsulation and structural stabilization

Ternary composite systems formed by lactoferrin (LF), sodium alginate (Alg), and Fe(II) were designed to investigate their potential as an iron delivery platform with enhanced protein stability. The ternary LF-Alg-Fe (LAF) composites demonstrated distinct structures depending on the LF to Alg ratio and the Fe(II) concentrations. At an LF to Alg ratio of 8:2 and final Fe concentrations between 20-30 mM, the system formed complexes stabilized by electrostatic interactions. Whereas Alg-rich formulations formed hydrogels stabilized by Alg-Fe(II) egg-box cross-linking. Rheological analysis and swelling behavior indicated a higher mechanical strength in LF-rich complexes and stronger network integrity in Alg-rich hydrogels, while intermediate LF/Alg ratios showed weaker structures overall. Fourier-transform infrared spectroscopy (FTIR) spectra showed no changes in functional groups or polymer structures after composite formation, confirming composite formation via non-covalent interactions. Thermal studies indicated that these ternary systems improved LF stability, evidenced by preserved secondary structure after heating using circular dichroism (CD), and an increased denaturation temperature compared with free LF in differential scanning calorimetry (DSC). In addition, in LF-rich formulations the Fe(II) release in aqueous solution was [~]50% while in Alg-rich formulations it was much lower (< 10%). LF-Alg-Fe composites exhibit distinct structures governed by protein-polysaccharide interactions and iron-mediated cross-linking, providing a potential strategy for protein stabilization and iron fortification in food systems.

biochemistry↗

Composition and Functional Properties of Hemp Seed Protein Isolates from Various Hemp Cultivars

Hemp seed protein isolates (HPI) were extracted from the seeds of seven commercial hemp cultivars, a Cornell breeding line, and a commercial hemp heart product. The composition and functional properties of the resulting HPI were investigated. HPI were of high protein purity >96% and contained various ratios of the major protein classes edestin, vicilin, and albumin, depending on the source. Protein solubility varied across HPI, and there was a positive correlation between greater levels of vicilin and albumin and improved solubility. The isoelectric points of HPI ranged from 5.50 to 5.94 but did not show significant effects associated with major protein class ratio. Significant differences in HPI foam capacity (52.9-84.9%), foam stability (68.1-89.4%), water holding capacity (0.83-1.05 g water/g protein isolate), and oil holding capacity (1.28-1.81 g oil/g protein isolate) were observed. In general, the emulsions generated from HPI performed poorly in terms of emulsifying activity, stability, and emulsion particle size. The ratio of edestin, vicilin, and albumin was found to play a major role in HPI functionality, suggesting that certain hemp cultivars may be better suited for generating protein ingredients that can functionalize plant-based foods.

biochemistry↗