Freeze, spray, and vacuum dried Camelina sativa protein powders and their physicochemical and functional properties

Abstract

The objective of this study was to examine the effect of different drying methods on the physicochemical and functional properties of camelina protein. Camelina protein was extracted using the alkaline extraction and isoelectric precipitation method and subsequently dried by freeze, spray, and vacuum-drying. The protein contents of camelina protein powders ranged between 62.5 and 64.1 g/100 g (dry basis). Glutamic acid was the most dominant amino acid for spray-dried and vacuum-dried proteins, while proline was for freeze-dried camelina protein. Camelina proteins had a peak denaturation temperature between 100.5 and 104.3 ◦C. The surface hydrophobicity of freeze-dried camelina protein (5.8 µg/mg) was lower than others (9.1–19.1 µg/mg). The spraydried protein showed the highest water-holding capacity (2.9 g/g), emulsion activity (0.53 mL/mL) and stability (0.96 mL/mL), as well as foaming capacity (0.48 mL/mL) and stability (0.92 mL/mL) among camelina proteins. Moreover, spray-dried camelina protein formed gel at a lower concentration (10 %). Consequently, camelina protein powders produced by different drying methods demonstrated different physicochemical and functional properties.