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Peer-reviewedCC BYFood chemistry: X

Synergistic Alcalase-papain hydrolysis of egg white protein: enhancing structural unfolding, antioxidant activity, and gastrointestinal stability.

  • Jialei Shi1
  • Xianzhen Li1
  • Xunyu Song2,3,4
  • Siqi Wang1
4 affiliations
  1. 1School of Biological Engineering, Dalian Polytechnic University, Qinggongyuan 1, Dalian, Liaoning, China.
  2. 2State 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.
  3. 3Dalian Key Laboratory for Precision Nutrition, Collaborative Innovation Center of Seafood Deep Processing, Academy of Food Interdisciplinary Science, Dalian Polytechnic University, Dalian, Liaoning, China.
  4. 4Dalian Key Laboratory for Precision Nutrition, Dalian Polytechnic University, Dalian, Liaoning, China.
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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.

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Cite

BibTeXRIS
BibTeX
@article{shi2026synergistic,
  title = {{Synergistic Alcalase-papain hydrolysis of egg white protein: enhancing structural unfolding, antioxidant activity, and gastrointestinal stability.}},
  author = {Jialei Shi and Xianzhen Li and Xunyu Song and Siqi Wang},
  journal = {Food chemistry: X},
  year = {2026},
  month = oct,
  doi = {10.1016/j.fochx.2026.104581},
  url = {https://europepmc.org/article/MED/42898412},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Synergistic Alcalase-papain hydrolysis of egg white protein: enhancing structural unfolding, antioxidant activity, and gastrointestinal stability.
AU  - Jialei Shi
AU  - Xianzhen Li
AU  - Xunyu Song
AU  - Siqi Wang
PY  - 2026
DA  - 2026/10/08
JO  - Food chemistry: X
DO  - 10.1016/j.fochx.2026.104581
UR  - https://europepmc.org/article/MED/42898412
AB  - 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.
SN  - 2590-1575
ER  -