Physicochemical and Antioxidant Properties of Industrial Hemp Seed Protein Isolate Treated by High-Intensity Ultrasound
Abstract
Ultrasound is one of the non-thermal, green, and novel technologies used to functionalize plant proteins. We recently determined the optimum conditions of high-intensity ultrasound (HIUS) treatment for maximum solubility and investigated the functional properties of hemp seed protein isolate (HSPI) under the optimal conditions. In this study, we analyzed changes in primary, secondary, and tertiary structures, physical microstructures, thermal stability, and antioxidant capacity of ultrasound-applied hemp protein isolate (HSPI-HIUS). The free SH group content (+59%) and zeta potential (+25%) increased upon ultrasound treatment. The electrophoretic protein patterns of HSPI showed no significant change after HIUS treatment. The FTIR spectrum revealed the wavenumber shifts in Amid 1 and 2 regions of protein. The denaturation temperature and the ratio of β-structure increased after sonication. Antioxidant properties of hemp seed protein isolates were increased by 38% by ultrasound treatment. The obtained data in this study showed that HIUS treatment would be promising for improving the functional, physicochemical, and antioxidant properties of HSPI.
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There is a need for sustainable alternative protein sources from plant matrices due to increasing demand for animal-based dietary proteins.
“Due to the increasing demand for animalbased dietary proteins, the need for sustainable alternative protein sources from plant matrices such as legumes, cereals, oilseeds, flowers, nuts, and others has been identified [12].”
From Functional and Bioactive Characterization of Hemp Cake Proteins and Polyphenols from Non-Psychoactive Cannabis sativa (2025) · cites this paper as [12]
Cites
Physicochemical and Functional Properties of Hemp ( <i>Cannabis sativa</i> L.) Protein Isolate
Tang, C.-H., Ten, Z., Wang, X.-S., & Yang, X.-Q. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0619176 · Cited by 405 · see citing works
Setti, L., Samaei, S. P., Maggiore, I., Nissen, L., Gianotti, A., & Babini, E. (2020) · Food and Bioprocess Technology · doi:10.1007/s11947-020-02550-6 · Cited by 20 · cited 1× · see citing works
“In recent years, enzymatic [6], chemical [7], and thermal [8] modification techniques have been applying to overcome these challenges of hemp seed protein.”
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Karabulut, G., Purkiewicz, A., & Goksen, G. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13372 · Cited by 85 · see citing works
Self-citationKarabulut, G., Kahraman, O., Pandalaneni, K., Kapoor, R., & Feng, H. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127240 · Cited by 51 · see citing works
Self-citationQuinteros, M., Wilcaso, P., Ribadeneira, C., & Vilcacundo, E. (2025) · Processes · doi:10.3390/pr13103184 · Cited by 3 · see citing works
- Authors
- Karabulut, G., Feng, H., & Yemiş, O.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Sakarya University (TR)
- Corresponding author
- Yemiş, Oktay
- Venue
- Plant Foods for Human Nutrition
- Published
- 2022-10-13
- Volume
- 77
- Issue
- 4
- Pages
- 577-583
- ISSN
- 0033-5134 (ISSN-L)
- 0921-9668
- 1573-9104
- OpenAlex
- W4304892213
- Cited by
- 60
- References
- 2
- Citations by year
- 2026: 6 · 2025: 24 · 2024: 19 · 2023: 8 · 2022: 3
- FWCI
- 7.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Plant Foods for Human Nutrition (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Sakarya Üniversitesi (2020-7-25-24)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Inactivation Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Keywords
- high-intensity ultrasound, protein functionalization, protein solubility, protein secondary structure, protein tertiary structure, thermal stability, antioxidant capacity, free thiol groups, zeta potential, protein denaturation, non-thermal processing
- MeSH terms
- Antioxidants, Cannabis, Particle Size, Plant Proteins, Seeds
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