Cited by 100Proteins in Food SystemsAgricultural and Biological ResearchFood composition and properties

Effects of ultrasound-assisted α-amylase degradation treatment with multiple modes on the extraction of rice protein

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Yang, Xue, Li, Yunliang, Li, Suyun, Oladejo, Ayobami Olayemi, Wang, Yucheng, Huang, Shanfen, Zhou, Cunshan, Ye, Xiaofei +2 more·2018·Ultrasonics Sonochemistry

Abstract

The effects of ultrasound-assisted α-amylase degradation (UAD) treatment with multiple modes on the extraction of rice protein (RP) from rice dreg powder were studied. The results showed that UAD treatment increased protein extraction rate significantly (p<0.05) compared to that of α-amylase degradation treatment and control. Among all the ultrasound mode treatments researched in this paper, sequential frequency ultrasound treatment presented higher protein extraction rate compared to that of simultaneous or single frequency ultrasound treatment. The highest protein extraction rate was obtained under 20/35kHz of sequential frequency UAD treatment with the protein extraction rate of 89.58% and protein purity of 92.99%. The test and analysis of fourier transform infrared spectroscopy, ultraviolet-visible spectroscopy, starch content, non-protein nitrogen content, SH and SS content, surface hydrophobicity, amino acids content and proteins characteristics were studied to reveal the mechanism of UAD on the protein extraction effect. After treated with UAD, the starch-protein agglomerates disintegrated completely, moreover, protein advanced structure was changed to some extent and the disulfide bond was partially broken, but the main chain structure (peptide chain), specificity of protein and amino acid composition were not obviously changed. Consequently, the structure modified RP extracted by UAD treatment presented higher solubility, emulsifying activity and foaming capacity, which was beneficial for the application of RP. In conclusion, UAD treatment is an effective method for maximizing extraction rate, purity and modifying properties of extracted protein.

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References 48 · Cited by 100

Research works printed but not linked: 3

  1. S. Wang, Study on enzymatic modigication technology of rice dreg protein by protease complex, Thesis Nanchang University, Jiangxi, China, 2015.
  2. C. Ju, Study on product of starch interacted with collagen and its digestibility properties, Thesis South China University of Technology, Guangzhou, China, 2011.
  3. R. Yan, Research on the combined structure and separation mechanism of starch and protein in corn, Thesis Shenyang University, Shenyang, China, 2016.

Authors
Yang, X., Li, Y., Li, S., Oladejo, A. O., Wang, Y., Huang, S., Zhou, C., Ye, X., Ma, H., & Duan, Y.
Affiliations
Jiangsu University (CN)
Corresponding author
  • Li, Yunliang
  • Ma, Haile
Venue
Ultrasonics Sonochemistry
Publisher
Elsevier BV
Published
2018-01
Volume
40
Issue
Pt A
Pages
890-899
ISSN
1350-4177 (ISSN-L)
OpenAlex
W2748677838
Cited by
100
References
48
Citations by year
2026: 11 · 2025: 12 · 2024: 13 · 2023: 18 · 2022: 14 · 2021: 13 · 2020: 10 · 2019: 5 · 2018: 4
FWCI
5.84
Type
journal article
Language
en
Open access
Locations
  • Ultrasonics Sonochemistry (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Funders
  • National Key R&D Program (2016YFD040030351)
  • National Natural Science Foundation (31701538, 31471698)
  • Scientific Innovation Research of College Graduate in Jiangsu Province (KYLX16_0916)
  • Policy Guidance Program (BY2016072-03)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Agricultural and Biological Research
  • Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
Keywords
rice protein, protein extraction, protein solubility, emulsifying activity, foaming capacity, protein structure modification
MeSH terms
Ultrasonic Waves, alpha-Amylases, Amino Acids, Enzyme Stability, Chemical Fractionation, Plant Proteins, Oryza, Hydrophobic and Hydrophilic Interactions, Proteolysis

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