Cited by 212Protein Hydrolysis and Bioactive PeptidesProteins in Food SystemsProtein Structure and Dynamics

Effects of ultrasound pretreatment with different frequencies and working modes on the enzymolysis and the structure characterization of rice protein

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Yang, Xue, Li, Yunliang, Li, Suyun, Oladejo, Ayobami Olayemi, Ruan, Siyu, Wang, Yucheng, Huang, Shanfen, Ma, Haile·2017·Ultrasonics Sonochemistry

Abstract

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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Crossref · 10.1016/j.ultsonch.2017.02.026

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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
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
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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