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Updated: Jun 20, 2026

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
Improved amino acid bioaccessibility, digestibility, and bioactivity in a soy-yeast dual protein system
Pengpeng Sun1, Yuan Yuan1, Xi Cheng1
1College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China; Key Laboratory of Environment Correlative Dietology (Huazhong Agricultural University), Ministry of Education, PR China; Hubei Key Laboratory of Fruit & Vegetable Processing & Quality Control (Huazhong Agricultural University), Wuhan, Hubei 430070, PR China.
Abstract:
Soy protein isolate (SPI) is a sustainable alternative to animal proteins, but constrained by imbalanced indispensable amino acid (IAA) profile and limited digestibility. In this study, dual proteins were constructed by SPI and yeast protein (YP). YP inclusion increased lysine and sulfur-containing amino acids (SAA) contents. At a 70:30 SPI-YP ratio, in vitro IAA bioaccessibility reached 97.8%, surpassing single SPI and YP. A 50:50 ratio obtained the most balanced absorbable IAA pattern and highest SAA score after digestion. Digesta exhibited improved antioxidant activity and ratio-dependent pancreatic lipase inhibition. Functionally, higher YP proportions decreased solubility and interfacial activity but maintained emulsion and foam stability. Structurally, with increasing YP, aggregation and zeta potential decreased, accompanied by conformational rearrangement. After gastric digestion, peptides (<20 kDa) appeared, β-sheet decreased, which were indistinguishable after intestinal digestion. These results underscored the potential of hybrid plant-microbe proteins to deliver high nutritional quality and bioactivity.
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