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This study focused on the influence of convection (at 40 °C and 50 °C) and freeze drying on functionality, structural properties and antioxidant potential of sunflower meal protein (SP m ) and hydrolysate (SPH m ). Likened to the respective convectively-dried isolates, lyophilized SP m  and SPH m  showed higher dispersibility and water binding efficacy, but lower oil binding efficacy (buttressed by surface hydrophobicity results) ( p  &lt; 0.05). The alterations in sulfhydryl clusters and disulfide bridges due to convection drying (under varied temperatures) implied limited unfolding of SP m  and SPH m  structure and reduction in intermolecular interactions. Moreover, fluorescent intensity and deconvoluted Fourier transform infrared (FTIR) spectroscopy illustrated that convectively-dried (CD) preparations, considerably CDSPH m , possessed more flexible/movable secondary structures over freeze-dried isolates. Topographical study indicated that dehydrated SPH m-s  had irregular small particles with partly destroyed/splitted micropores, suggesting disruption in the noncovalent bonds between SPH m-s  molecules. Furthermore, isolates from the freeze drying process, notably lyophilized hydrolysate, showed higher antioxidative (DPPH scavenging, ABTS and reducing power) potential over the convectively-dried samples, supported by the analysis of amino acids composition. The current investigation could help the pharmacological and/or food industry to develop new therapeutic product and/or functional food from lyophilized isolates.

drying technology

Functional, conformational, topographical, and antioxidative properties of convectively- and freeze-dried sunflower protein and hydrolysate: a comparative investigation