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Freeze-Drying-Induced Hydrophobic Aggregation Limits the Redissolubility of Spirulina Protein: Limiting Factors and Solubilization Mechanism

delete2026-08-08
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PRE
AI
J
Jie Zhou
H
Hao Chen
Y
Yingwen Lan
J
Jinjin Liu
C
Chen Zhang *
DOI：10.1016/j.jfoodeng.2026.113283delete
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Abstract

Abstract

En 中文
• Stepwise alkali-ultrasound yields 93% Spirulina protein with subunits intact. • Freeze-drying induces rigid aggregates, limiting SPE redissolubility to ∼65%. • Hydrophobic interactions dominate; physical optimization fails to reverse aggregates. • Cascade synergistic mechanism achieves 96% protein redissolubility. • Disrupting hydrogen/disulfide bonds pre-exposes hydrophobic regions for precise disruption.
Keywords:
Spirulina protein
freeze-drying
redissolubility
hydrophobic interaction
synergistic solubilization

Journal

Journal of Food Engineering cover
Journal of Food Engineering
IF:
5.8
Papers:
1.0W
Citations:
3.3W

Organization

F
fuzhou university
Scholars:
3.1W
Papers: 2.1W
Citations: 31
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