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<p>Potato protein (PP) has superior nutritional value, which makes it a promising alternative to egg protein. However, its utilization in the food industry is limited because of its unsatisfactory physicochemical properties. The aim of this study was to solve this problem by improving the functional properties of PP through glutaminase deamidation. Compared with that of control group, the solubility of the 0.05 U/mL deamidation sample increased from 0.68&#xa0;g/mL to 1.31&#xa0;g/mL (<i>p</i> &lt; 0.05), and its TSI value remained at a relatively low level (&lt; 0.2). Zeta potential particle size analysis revealed that the particle size of PP decreased after deamidation and the particles were more uniform. Moreover, the results of spectral analysis indicated that the deamidation of glutaminase led to the transformation of the ordered secondary structure of proteins (from 71% to 49%) into a disordered structure, resulting in a looser structure. Endogenous fluorescence and atomic force analysis revealed that the protein molecular structure increased and that polarity of the tryptophan microenvironment increased. Our results indicated that glutaminase treatment provides a promising strategy for improving the functionality of potato protein.</p> Graphical Abstract <p></p>

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Effect of glutaminase on emulsifying function and molecular structure of potato protein

  • 期刊论文

  • 发表日期：

    2025年11月13日

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  • Xingli Liu,
  • Yaru Yuana,
  • Boren Yu,
  • Chenhui Ren,
  • Hongwei Wang,
  • Huishan Shen,
  • Weimin Kang,
  • Hua Zhang,
  • Yanyan Zhang

摘要

Potato protein (PP) has superior nutritional value, which makes it a promising alternative to egg protein. However, its utilization in the food industry is limited because of its unsatisfactory physicochemical properties. The aim of this study was to solve this problem by improving the functional properties of PP through glutaminase deamidation. Compared with that of control group, the solubility of the 0.05 U/mL deamidation sample increased from 0.68 g/mL to 1.31 g/mL (p < 0.05), and its TSI value remained at a relatively low level (< 0.2). Zeta potential particle size analysis revealed that the particle size of PP decreased after deamidation and the particles were more uniform. Moreover, the results of spectral analysis indicated that the deamidation of glutaminase led to the transformation of the ordered secondary structure of proteins (from 71% to 49%) into a disordered structure, resulting in a looser structure. Endogenous fluorescence and atomic force analysis revealed that the protein molecular structure increased and that polarity of the tryptophan microenvironment increased. Our results indicated that glutaminase treatment provides a promising strategy for improving the functionality of potato protein.

Graphical Abstract