Effects of multi-frequency ultrasound pretreatment under low power density on the enzymolysis and the structure characterization of defatted wheat germ protein
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The effects of ultrasonic frequency mode, power density, pretreatment time and other parameters under low power density on the degree of hydrolysis (DH) of defatted wheat germ protein (DWGP) and angiotensin-I-converting enzyme (ACE) inhibitory activity of DWGP hydrolysate were studied in this research. Ultraviolet-visible (UV-Vis) spectra, free sulfhydryl (SH), disulfide bond (SS), surface hydrophobicity and hydrophobic protein content of ultrasound-pretreated protein and hydrophobic amino acid (HAA) content of alcalase-hydrolysate of DWGP were measured under optimized ultrasonic condition. The ultrasonic frequency mode with dual-fixed frequency combination of 28/40kHz showed higher ACE inhibitory activity of DWGP hydrolysate compared with that of other ultrasound frequency modes and all the ultrasonic frequency combinations involving in 28kHz showed higher ACE inhibitory activity. Under the dual-fixed frequency ultrasound mode of 28/40kHz, ultrasonic power density of 60W/L, pretreatment time of 70min, temperature of 60°C and substrate concentration of 60g/L, the ACE inhibitory activity of DWGP hydrolysate was the highest with its value of 74.75% (increased by 62.30% compared to control). However, all the ultrasonic pretreatment did not increase the DH of DWGP significantly (p>0.05). The changes in UV-Vis spectra, SH and SS groups, surface hydrophobicity and hydrophobic protein content indicated that the structure of DWGP unfolded after ultrasound pretreatment. The HAA content of hydrolysate from the pretreated DWGP increased significantly (p<0.05). The results proved that ultrasound pretreatment loosed the protein structure and exposed more HAA residues of protein to be attacked easily by alcalase. This resulted in the increase in the HAA content which related to the ACE inhibitory activity.
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High-intensity ultrasonic waves can modify proteins, resulting in functional alterations.
“When subjected to high-intensity ultrasonic waves, proteins can undergo modifications that result in functional alterations.”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [31]
Ultrasonic treatment disrupts interactions between protein molecules, leading to protein unfolding and increased exposure of protein surfaces.
“The disruptive effect of ultrasonic treatment on the interactions between protein molecules can lead to protein unfolding, thereby increasing the exposure of protein surfaces. This unfolding phenomenon induced by ultrasonic treatment has the potential to impact the functionality of proteins [31].”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [31]
Under dual-fixed frequency ultrasonic mode of 28/40 kHz, power density 60 W/L, pretreatment time 70 min, temperature 60 °C, substrate concentration 60 g/L, DWGP hydrolysate exhibited highest ACE inhibitory activity.
“Under the dual-fixed frequency ultrasonic mode of 28/40 kHz, an ultrasonic power density of 60 W/L, a pretreatment time of 70 min, a temperature of 60 °C and a substrate concentration of 60 g/L, the DWGP hydrolysate exhibited the highest ACE inhibitory activity.”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [31]
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“Also, Xue et al. [31] examined the influence of ultrasonic frequency mode, power density, pretreatment time, and other parameters at low power density on the degree of hydrolysis (DH) of defatted wheat germ protein (DWGP) and the angiotensin-I-converting enzyme (ACE) inhibitory activity of DWGP…”
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- Authors
- Yang, X., Li, Y., Li, S., Oladejo, A. O., Wang, Y., Huang, S., Zhou, C., Wang, Y., Mao, L., Zhang, Y., Ma, H., & Ye, X.
- Affiliations
- Jiangsu University (CN)
- Zhengzhou University of Light Industry (CN)
- Corresponding author
- Li, Yunliang
- Ma, Haile
- ORCID
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 38
- Pages
- 410-420
- ISSN
- 1350-4177 (ISSN-L)
- OpenAlex
- W2594864725
- Cited by
- 121
- References
- 43
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 9 · 2023: 15 · 2022: 15 · 2021: 18 · 2020: 18 · 2019: 11 · 2018: 8 · 2017: 5
- FWCI
- 4.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Ultrasonics Sonochemistry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Graduate Research and Innovation Projects of Jiangsu Province (KYLX16_0916)
- National Natural Science Foundation of China (31471698)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- ultrasonic pretreatment, multi-frequency ultrasound, low power density, proteolysis, alcalase hydrolysate, angiotensin-converting enzyme inhibition, degree of hydrolysis, disulfide bonds, free sulfhydryl groups, surface hydrophobicity, hydrophobic amino acids, dual-frequency ultrasound
- MeSH terms
- Ultrasonic Waves, Angiotensin-Converting Enzyme Inhibitors, Disulfides, Fatty Acids, Hydrolysis, Plant Proteins, Surface Properties, Triticum, Hydrophobic and Hydrophilic Interactions, Proteolysis
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