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<p>Bee pollen is a high-protein superfood, but its rigid multilayered structure (exine and intine layers) hinders efficient protein extraction. Therefore, disruption of this multilayered structure is necessary to enhance the protein yield and functionality. Accordingly, the current research compared ultrasound (US), pectinase enzyme (PE), and their synergistic action (US-PE) as pre-treatment techniques for cell wall disruption of bee pollen and its subsequent protein extraction. Furthermore, the research investigated the effect of these pre-treatments on the physical, structural, rheological, and toxicological characteristics of extracted bee pollen protein isolates (BPPIs). The results demonstrated that among the different pre-treatments employed, US-PE exhibited the most prominent effect on BPPI. US-PE-BPPI showed reduced bulk (0.18 ± 0.01&#xa0;g/mL) and tapped densities (0.28 ± 0.03&#xa0;g/mL) as compared with untreated BPPI (0.41 ± 0.01&#xa0;g/mL), which indicates alterations in the protein structure. US-PE-BPPI is further characterized by a higher zeta potential value (− 34.4 ± 0.7&#xa0;mV), and increased exposure of free (16.13 ± 0.11&#xa0;µmol/g) and total sulfhydryl groups (22.03 ± 0.10&#xa0;µmol/g). This observed variation is ascribed to the dual effect of cavitation-induced shear forces and hydrolysis, which facilitated protein unfolding and conformational rearrangements. Circular dichroism analysis revealed decreased α-helix and increased β-sheet content of US-PE-BPPI which signifies structural modification in proteins. Rheological analysis illustrated predominant elastic behaviour (tan δ &lt; 1), reflecting the formation of stronger gel protein matrix. In addition, cytotoxicity results confirmed the non-toxic nature of all BPPIs, with US-PE-BPPI exhibiting the highest in vitro digestibility. The research findings support the utilization of pre-treatment-induced BPPI in functional foods of high nutritional value.</p>

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Effect of Ultrasound-Assisted Enzymatic Pre-treatment on Conformational, Rheological, and Toxicological Properties of Bee Pollen Protein Isolates for Application in Food Systems

  • 期刊论文

  • 发表日期：

    2026年4月13日

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  • Anamika Sharma,
  • Avinash Thakur,
  • Vikas Nanda

摘要

Bee pollen is a high-protein superfood, but its rigid multilayered structure (exine and intine layers) hinders efficient protein extraction. Therefore, disruption of this multilayered structure is necessary to enhance the protein yield and functionality. Accordingly, the current research compared ultrasound (US), pectinase enzyme (PE), and their synergistic action (US-PE) as pre-treatment techniques for cell wall disruption of bee pollen and its subsequent protein extraction. Furthermore, the research investigated the effect of these pre-treatments on the physical, structural, rheological, and toxicological characteristics of extracted bee pollen protein isolates (BPPIs). The results demonstrated that among the different pre-treatments employed, US-PE exhibited the most prominent effect on BPPI. US-PE-BPPI showed reduced bulk (0.18 ± 0.01 g/mL) and tapped densities (0.28 ± 0.03 g/mL) as compared with untreated BPPI (0.41 ± 0.01 g/mL), which indicates alterations in the protein structure. US-PE-BPPI is further characterized by a higher zeta potential value (− 34.4 ± 0.7 mV), and increased exposure of free (16.13 ± 0.11 µmol/g) and total sulfhydryl groups (22.03 ± 0.10 µmol/g). This observed variation is ascribed to the dual effect of cavitation-induced shear forces and hydrolysis, which facilitated protein unfolding and conformational rearrangements. Circular dichroism analysis revealed decreased α-helix and increased β-sheet content of US-PE-BPPI which signifies structural modification in proteins. Rheological analysis illustrated predominant elastic behaviour (tan δ < 1), reflecting the formation of stronger gel protein matrix. In addition, cytotoxicity results confirmed the non-toxic nature of all BPPIs, with US-PE-BPPI exhibiting the highest in vitro digestibility. The research findings support the utilization of pre-treatment-induced BPPI in functional foods of high nutritional value.