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Covalent binding of ultrasound-treated japonica rice bran protein to catechin: Structural and functional properties of the complex

Guo, Yanfei, Wang, Minghao, Xing, Kaiwen, Pan, Mingzhe, Wang, Liqi·2023·Ultrasonics Sonochemistry
DOI 10.1016/j.ultsonch.2023.106292PMC PMC9868872
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  • Protein unfolding and exposure of hydrophilic groups outweighed limited covalent crosslinking or oxidation, resulting in an overall increase in solubility.

    “This suggests that protein unfolding and exposure of hydrophilic groups outweighed limited covalent crosslinking or oxidation, resulting in an overall increase in solubility (Guo et al., 2023; Wang et al., 2023; Zhu et al., 2025).”

    From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Guo et al., 2023

  • The increase in SH content indicates that previously buried sulfhydryl groups became exposed due to protein unfolding.

    “The increase in SH content indicates that previously buried sulfhydryl groups became exposed due to protein unfolding (Guo et al., 2023; Wang, Yang, et al., 2022).”

    From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Guo et al., 2023

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Cited by

Sorted by citations

Authors
Guo, Y., Wang, M., Xing, K., Pan, M., & Wang, L.
Venue
Ultrasonics Sonochemistry
Publisher
Elsevier BV
Published
2023-02
Volume
93
Pages
106292
ISSN
1350-4177
DOI
10.1016/j.ultsonch.2023.106292
PMC
PMC9868872
Cited by
34
References
0
Language
en
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