{
  "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.",
  "abstract_shown": true,
  "affiliations": [
    "Hainan Engineering Center of Coconut Further Processing, Coconut Research Institute, Chinese Academy of Tropical Agricultural Sciences, Wenchang 571339, China",
    "College of Modern Agriculture and Bioengineering, Shangluo University, Shangluo 726000, China"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 3,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Xiaoyan Liu"
    },
    {
      "affs": [
        0
      ],
      "name": "Fuming Deng"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Yufeng Zhang",
      "orcid": "0000-0002-9409-468X"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/d6bhk4kjsvm69.bib",
  "cited_by": 0,
  "doi": "10.3390/molecules31203613",
  "fulltext_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13707485/?tool=EBI",
  "id": "d6bhk4kjsvm69",
  "issns": [
    "1420-3049"
  ],
  "landing_url": "https://www.mdpi.com/1420-3049/31/20/3613",
  "language": "eng",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1106|Proteins in Food Systems"
    ]
  ],
  "openalex": "W7221536041",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13707485/pdf/?tool=EBI",
  "pmcid": "PMC13707485",
  "pmid": null,
  "published": "2026-10-01",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/d6bhk4kjsvm69.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:42Z",
      "native_id": "10.3390/molecules31203613",
      "source": "crossref",
      "url": "https://www.mdpi.com/1420-3049/31/20/3613"
    },
    {
      "first_seen": "2026-10-30T12:21:40Z",
      "native_id": "PMC:PMC13707485",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13707485"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "issn:1420-3049",
      "subfield": "general"
    }
  ],
  "title": "Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties",
  "title_text": "Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:21:40Z",
  "url": "https://research.draconitic.com/paper/d6bhk4kjsvm69",
  "venue": "Molecules",
  "versions": []
}