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. 2022 Feb 4;27(3):1059.
doi: 10.3390/molecules27031059.

Physicochemical and Functional Properties of 2S, 7S, and 11S Enriched Hemp Seed Protein Fractions

Comfort F Ajibola  1 , Rotimi E Aluko  1
Affiliations

Physicochemical and Functional Properties of 2S, 7S, and 11S Enriched Hemp Seed Protein Fractions

Comfort F Ajibola et al. Molecules. .

Abstract

The hemp seed contains protein fractions that could serve as useful ingredients for food product development. However, utilization of hemp seed protein fractions in the food industry can only be successful if there is sufficient information on their levels and functional properties. Therefore, this work provides a comparative evaluation of the structural and functional properties of hemp seed protein isolate (HPI) and fractions that contain 2S, 7S, or 11S proteins. HPI and protein fractions were isolated at pH values of least solubility. Results showed that the dominant protein was 11S, with a yield of 72.70 ± 2.30%, while 7S and 2S had values of 1.29 ± 0.11% and 3.92 ± 0.15%, respectively. The 2S contained significantly (p < 0.05) higher contents of sulfhydryl groups at 3.69 µmol/g when compared to 7S (1.51 µmol/g), 11S (1.55 µmol/g), and HPI (1.97 µmol/g). The in vitro protein digestibility of the 2S (72.54 ± 0.52%) was significantly (p < 0.05) lower than those of the other isolated proteins. The intrinsic fluorescence showed that the 11S had a more rigid structure at pH 3.0, which was lost at higher pH values. We conclude that the 2S fraction has superior solubility, foaming capacity, and emulsifying activity when compared to the 7S, 11S, and HPI.

Keywords: albumin; amino acid composition; circular dichroism; functional properties; globulins; hemp seed; intrinsic fluorescence; protein digestibility.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript; or in the decision to publish the results.

Figures

Figure 1
Figure 1
SDS-PAGE of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S) under reducing (A) and non-reducing (B) conditions.
Figure 2
Figure 2
Intrinsic fluorescence intensity of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S).
Figure 3
Figure 3
Far-UV spectra of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S) at different pH values.
Figure 4
Figure 4
Near-UV spectra of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S) at different pH values.
Figure 5
Figure 5
pH-dependent changes in the solubility of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S).
Figure 6
Figure 6
Foam stability of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S) at different pH values. Bars with different letters have significantly different values (p < 0.05).
Figure 7
Figure 7
Emulsion stability of hemp seed protein isolate (HPI) and fractions (2S, 7S, and 11S) at different pH values. Bars with different letters have significantly different values (p < 0.05).
See this image and copyright information in PMC

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