Effects of ultrasound pretreatment with different frequencies and working modes on the enzymolysis and the structure characterization of rice protein
Open accessAbstract
The effects of ultrasound pretreatment with different frequencies and working modes, including mono-frequency ultrasound (MFU), dual-frequency ultrasound (DFU) and tri-frequency ultrasound (TFU), on the degree of hydrolysis (DH) of rice protein (RP) and angiotensin-I-converting enzyme (ACE) inhibitory activity of RP hydrolysate were investigated. Ultraviolet-visible (UV) spectroscopy, fourier transform infrared (FTIR) spectroscopy, surface hydrophobicity and scanning electron microscopy (SEM) of RP pretreated with ultrasound were measured. The results showed that ultrasound pretreatment did not increase DH of RP significantly (p>0.05). However, all the ultrasound pretreatment increased the ACE inhibitory activity of RP hydrolysate significantly (p<0.05). The MFU of 20kHz showed higher ACE inhibitory activity compared to that of other MFU. The ACE inhibitory activity of sequential DFU was higher than that of simultaneous with the same frequency combination. Sequential TFU of 20/35/50kHz produced the highest increase in ACE inhibitory activity in contrast with other ultrasound frequencies and working modes. All the results under ultrasound pretreatment showed that ultrasound frequencies and working modes were of great effect on the ACE inhibitory activity of RP. The changes in UV-Vis spectra and surface hydrophobicity indicated the unfolding of protein and exposure of hydrophobic groups by ultrasound. The FTIR analysis showed that all the ultrasound pretreatment with different frequencies and working modes decreased α-helix, β-turn content and increased β-sheet, random coil content of RP. The SEM results indicated that ultrasound pretreatment resulted in the deformation of RP. In conclusion, the frequency selection of ultrasound pretreatment of RP is essential for the preparation of ACE inhibitory peptide.
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Ultrasonic pretreatment of rice protein can lead to spreading out of the α-helix region and shaping of β-sheet.
“Xue et al. [33] reported that ultrasonic pretreatment of rice protein can lead to spreading out of the α-helix region and the shaping of β-sheet.”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [33]
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- Authors
- Yang, X., Li, Y., Li, S., Oladejo, A. O., Ruan, S., Wang, Y., Huang, S., & Ma, H.
- Affiliations
- Jiangsu University (CN)
- Corresponding author
- Li, Yunliang
- Ma, Haile
- ORCID
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 38
- Pages
- 19-28
- ISSN
- 1350-4177 (ISSN-L)
- OpenAlex
- W2591193029
- Cited by
- 212
- References
- 41
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 29 · 2023: 33 · 2022: 22 · 2021: 30 · 2020: 29 · 2019: 14 · 2018: 17 · 2017: 8
- FWCI
- 7.59
- 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 › Molecular Biology › Protein Structure and Dynamics
- Keywords
- rice protein, ultrasonic pretreatment, ultrasonic frequency, dual-frequency ultrasound, enzymatic hydrolysis, angiotensin-converting enzyme inhibition, ACE inhibitory peptides, protein secondary structure, protein unfolding, surface hydrophobicity, degree of hydrolysis
- MeSH terms
- Ultrasonic Waves, Hydrolysis, Peptidyl-Dipeptidase A, Plant Proteins, Oryza, Protein Structure, Secondary, Hydrophobic and Hydrophilic Interactions
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