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<p>The black bean protein isolate (BBPI) has attracted much attention in plant-based foods due to its superior amino acid composition and health functions, but its inherent functional properties cannot meet industrial production needs. Therefore, this study combined ultrasound and transglutaminase (TGase) cross-linking, systematically characterized the structural changes through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), fluorescence spectroscopy, fourier transform infrared spectrometer, scanning electron microscope and other methods, and analyzed their relationship with functional properties. The results showed that ultrasound pretreatment promoted the cross-linking between TGase and BBPI, resulting in an increase in β-sheet content, enhanced fluorescence intensity, moderate unfolding of protein structure, exposure of hydrophobic groups, and an increase in surface hydrophobicity to 27.13 × 10⁴. After the ultrasonic pretreatment, protein-protein interactions increase, forming a denser microstructure, thereby improving thermal stability, and the thermal denaturation temperature rises to 108.15 ℃. The particle size of the sample decreased to 79.50&#xa0;nm, and the absolute value of the zeta potential increased, thereby reducing particle settling and resulting in a decrease in turbidity to 0.088 and an increase in solubility to 38.62%. This study reveals the synergistic mechanism of ultrasound and TGase, provides a theoretical basis for the development of highly soluble BBPI powders and offers an efficient and safe protein composite modification strategy for the food industry.</p>

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Effects of ultrasonic pretreatment on the structure, solubility and thermal stability of transglutaminase cross-linked black bean protein isolate

  • 期刊论文

  • 发表日期：

    2025年8月20日

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  • Yuejiao Xing,
  • Yue San,
  • Bailiang Li,
  • Li Zheng

摘要

The black bean protein isolate (BBPI) has attracted much attention in plant-based foods due to its superior amino acid composition and health functions, but its inherent functional properties cannot meet industrial production needs. Therefore, this study combined ultrasound and transglutaminase (TGase) cross-linking, systematically characterized the structural changes through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), fluorescence spectroscopy, fourier transform infrared spectrometer, scanning electron microscope and other methods, and analyzed their relationship with functional properties. The results showed that ultrasound pretreatment promoted the cross-linking between TGase and BBPI, resulting in an increase in β-sheet content, enhanced fluorescence intensity, moderate unfolding of protein structure, exposure of hydrophobic groups, and an increase in surface hydrophobicity to 27.13 × 10⁴. After the ultrasonic pretreatment, protein-protein interactions increase, forming a denser microstructure, thereby improving thermal stability, and the thermal denaturation temperature rises to 108.15 ℃. The particle size of the sample decreased to 79.50 nm, and the absolute value of the zeta potential increased, thereby reducing particle settling and resulting in a decrease in turbidity to 0.088 and an increase in solubility to 38.62%. This study reveals the synergistic mechanism of ultrasound and TGase, provides a theoretical basis for the development of highly soluble BBPI powders and offers an efficient and safe protein composite modification strategy for the food industry.