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<p>This work aimed to evaluate the proteomic profile of a buffalo whey protein concentrate (BWPC) and its performance as an encapsulating agent for hydrophobic molecules, using α-tocopheryl acetate (TOC) as a model compound. To this end, BWPC was digested with trypsin and analyzed by liquid chromatography-mass spectrometry. In parallel, mixtures of BWPC and TOC were analyzed by fluorescence and FTIR spectroscopies, as well as in terms of encapsulation efficiency (EE) using ultrafiltration. In addition, the stability against harmful agents, both chemical (8&#xa0;M urea) and physical (UVA radiation and heating at 50&#xa0;°C), was also evaluated. The proteomic profile of BWPC consisted of 29 proteins and peptides according to the bioinformatic analysis of the peptide fragments. Applying the Gene Ontology (GO) classification, the cellular anatomical entity was the main term for cellular components, while catalytic and binding activities were for molecular functions, and metabolic and cellular processes for biological processes. Besides, BWPC was able to encapsulate TOC with an EE of 86% through spontaneous molecular complexation (with free energy, ΔG ranging between − 23.0 to -18.5&#xa0;kJ·mol<sup>− 1</sup>) with a remarkable contribution of hydrophobic interactions. Upon complexation, the protein fraction underwent conformational changes. They were detected by shifts in the fluorescence spectra and infrared bands (amide II and III). Stability analysis of BWPC-TOC complexes against harmful chemical agents showed binding constant (K<sub>a</sub>) values from 2.84 × 10<sup>3</sup> to 1.08 × 10<sup>4</sup> M<sup>− 1</sup>, suggesting transient molecular interactions. Conversely, BWPC significantly enhanced TOC stability under physical stress, reducing its degradation rate. These findings expand current knowledge of the buffalo whey proteome and highlight BWPC’s potential as an encapsulating agent. This work also lays a foundation for future research on the mutual influence of hydrophobic bioactive compounds and BWPC proteins on stability, bioavailability, and functional properties in food systems.</p> Graphical abstract <p></p>

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Performance of water buffalo (Bubalus bubalis) whey proteins as innovative encapsulating agents for hydrophobic bioactive compounds

  • 期刊论文

  • 发表日期：

    2026年7月20日

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  • Leandro Fabián Bustos,
  • Franco Emanuel Vasile,
  • Oscar Edgardo Pérez

摘要

This work aimed to evaluate the proteomic profile of a buffalo whey protein concentrate (BWPC) and its performance as an encapsulating agent for hydrophobic molecules, using α-tocopheryl acetate (TOC) as a model compound. To this end, BWPC was digested with trypsin and analyzed by liquid chromatography-mass spectrometry. In parallel, mixtures of BWPC and TOC were analyzed by fluorescence and FTIR spectroscopies, as well as in terms of encapsulation efficiency (EE) using ultrafiltration. In addition, the stability against harmful agents, both chemical (8 M urea) and physical (UVA radiation and heating at 50 °C), was also evaluated. The proteomic profile of BWPC consisted of 29 proteins and peptides according to the bioinformatic analysis of the peptide fragments. Applying the Gene Ontology (GO) classification, the cellular anatomical entity was the main term for cellular components, while catalytic and binding activities were for molecular functions, and metabolic and cellular processes for biological processes. Besides, BWPC was able to encapsulate TOC with an EE of 86% through spontaneous molecular complexation (with free energy, ΔG ranging between − 23.0 to -18.5 kJ·mol− 1) with a remarkable contribution of hydrophobic interactions. Upon complexation, the protein fraction underwent conformational changes. They were detected by shifts in the fluorescence spectra and infrared bands (amide II and III). Stability analysis of BWPC-TOC complexes against harmful chemical agents showed binding constant (Ka) values from 2.84 × 103 to 1.08 × 104 M− 1, suggesting transient molecular interactions. Conversely, BWPC significantly enhanced TOC stability under physical stress, reducing its degradation rate. These findings expand current knowledge of the buffalo whey proteome and highlight BWPC’s potential as an encapsulating agent. This work also lays a foundation for future research on the mutual influence of hydrophobic bioactive compounds and BWPC proteins on stability, bioavailability, and functional properties in food systems.

Graphical abstract