{
  "abstract": "Egg white protein (EWP) is a promising source of bioactive peptides, but its compact structure limits enzymatic accessibility. This study compared single-protease hydrolysis using alcalase (Al) or papain (Pa) with composite alcalase-papain hydrolysis (Al-Pa) in terms of peptide production, structural modification, antioxidant activity, and digestive stability. Al-Pa achieved the highest hydrolysate yield (72.85%) and the largest proportion of peptides below 10 kDa (63.71%), including 26.34% below 3 kDa. Structurally, Al-Pa caused more extensive unfolding, hydrophobic group exposure, and microstructural reorganization than Al or Pa alone. During simulated gastrointestinal digestion, Al-Pa hydrolysates exhibited greater digestive stability, retained stronger DPPH radical-scavenging activity and high ABTS activity. The digested Al-Pa products also showed increases of 13.92% in branched-chain amino acids and 4.90% in hydrophobic amino acids, together with enrichment of sulfur-containing amino acids. These findings highlight the advantages of composite protease hydrolysis for producing EWP hydrolysates with sustained antioxidant functionality during digestion.",
  "abstract_shown": true,
  "affiliations": [
    "School of Biological Engineering, Dalian Polytechnic University, Qinggongyuan 1, Dalian, Liaoning, China.",
    "State Key Laboratory of Marine Food Processing and Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian, Liaoning, China.",
    "Dalian Key Laboratory for Precision Nutrition, Collaborative Innovation Center of Seafood Deep Processing, Academy of Food Interdisciplinary Science, Dalian Polytechnic University, Dalian, Liaoning, China.",
    "Dalian Key Laboratory for Precision Nutrition, Dalian Polytechnic University, Dalian, Liaoning, China."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Jialei Shi"
    },
    {
      "affs": [
        0
      ],
      "name": "Xianzhen Li"
    },
    {
      "affs": [
        1,
        2,
        3
      ],
      "name": "Xunyu Song"
    },
    {
      "affs": [
        0
      ],
      "name": "Siqi Wang"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/c47gbqcvs358x.bib",
  "cited_by": 0,
  "doi": "10.1016/j.fochx.2026.104581",
  "fulltext_url": "https://europepmc.org/articles/PMC13677955",
  "id": "c47gbqcvs358x",
  "issns": [
    "2590-1575"
  ],
  "landing_url": "https://europepmc.org/article/MED/42898412",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Protein Hydrolysis and Bioactive Peptides"
    ]
  ],
  "openalex": "W7220952351",
  "pdf_url": "https://europepmc.org/articles/PMC13677955?pdf=render",
  "pmcid": "PMC13677955",
  "pmid": "42898412",
  "published": "2026-10-08",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/c47gbqcvs358x.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:19:37Z",
      "native_id": "MED:42898412",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42898412"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Protein Hydrolysis and Bioactive Peptides",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Synergistic Alcalase-papain hydrolysis of egg white protein: enhancing structural unfolding, antioxidant activity, and gastrointestinal stability.",
  "title_text": "Synergistic Alcalase-papain hydrolysis of egg white protein: enhancing structural unfolding, antioxidant activity, and gastrointestinal stability.",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:19:37Z",
  "url": "https://research.draconitic.com/paper/c47gbqcvs358x",
  "venue": "Food chemistry: X",
  "versions": []
}