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Peer-reviewedCC BY 4.0Molecules

Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties

  • Xiaoyan Liu1
  • Fuming Deng1
  • Yufeng Zhang1,2
  1. 1Hainan Engineering Center of Coconut Further Processing, Coconut Research Institute, Chinese Academy of Tropical Agricultural Sciences, Wenchang 571339, China
  2. 2College of Modern Agriculture and Bioengineering, Shangluo University, Shangluo 726000, China
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Abstract

The heat-induced aggregation behavior of coconut globulin at pH 2.0 and 85 °C was investigated over a continuous heating period of 0–24 h, with a focus on the temporal evolution of protein structure and corresponding changes in techno-functional performance. The aggregation process exhibited three distinct stages: initial unfolding and dissociation (0–6 h), formation of β-sheet-enriched structures (6–12 h), and subsequent over-aggregation (12–24 h). Surface hydrophobicity reached its maximum at 20 h, foaming capacity peaked at 12 h, and emulsifying activity achieved its optimal value at 10 h. These time-dependent functional variations were closely correlated with progressive conformational rearrangement, peptide chain degradation, and interfacial structural changes. The results establish a time-resolved structure–function correlation for coconut globulin under acidic heating conditions, offering practical guidance for the processing of coconut protein as a plant-based functional ingredient.

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Cite

BibTeXRIS
BibTeX
@article{liu2026heatinduced,
  title = {{Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties}},
  author = {Xiaoyan Liu and Fuming Deng and Yufeng Zhang},
  journal = {Molecules},
  year = {2026},
  month = oct,
  doi = {10.3390/molecules31203613},
  url = {https://www.mdpi.com/1420-3049/31/20/3613},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties
AU  - Xiaoyan Liu
AU  - Fuming Deng
AU  - Yufeng Zhang
PY  - 2026
DA  - 2026/10/01
JO  - Molecules
DO  - 10.3390/molecules31203613
UR  - https://www.mdpi.com/1420-3049/31/20/3613
AB  - The heat-induced aggregation behavior of coconut globulin at pH 2.0 and 85 °C was investigated over a continuous heating period of 0–24 h, with a focus on the temporal evolution of protein structure and corresponding changes in techno-functional performance. The aggregation process exhibited three distinct stages: initial unfolding and dissociation (0–6 h), formation of β-sheet-enriched structures (6–12 h), and subsequent over-aggregation (12–24 h). Surface hydrophobicity reached its maximum at 20 h, foaming capacity peaked at 12 h, and emulsifying activity achieved its optimal value at 10 h. These time-dependent functional variations were closely correlated with progressive conformational rearrangement, peptide chain degradation, and interfacial structural changes. The results establish a time-resolved structure–function correlation for coconut globulin under acidic heating conditions, offering practical guidance for the processing of coconut protein as a plant-based functional ingredient.
SN  - 1420-3049
ER  -