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<p>Pea protein enriched flour was hydrolyzed using both proteases and amylases simultaneously, then it was heated to induce Maillard conjugation between proteins and polysaccharides. The resulting protein-starch conjugates were investigated for their structural, surface, and functional properties. SDS-polyacrylamide gel electrophoresis and scanning electron microscopy analyses showed the presence of different molecular species and altered microstructure in the conjugate preparations. The zeta potentials at pH 7 (− 20.6 to − 32.3 mV) and pH 10 (− 29.2 to − 36.6 mV) were more negative compared to pH 4 (0.2 to 8.6 mV), indicating higher exposure of ionized side chains. All trypsin-hydrolyzed protein-starch conjugates exhibited better foaming and emulsification properties compared to the papain-hydrolyzed protein-starch conjugates. Trypsin-hydrolyzed conjugates with a degree of hydrolysis (24%) showed the highest foam capacity (126.6%) at pH 7 and emulsion activity (24.0&#xa0;m²/g) at pH 10. In contrast, trypsin hydrolysates (21.7% degree of hydrolysis) exhibited increased emulsion stability (99.4%) at pH 7. It is commonly considered that high degree of hydrolysis results in complete unraveling of proteins, leading to lower functionality. The results of this study showed that conjugation between proteins and polysaccharides can counterbalance the negative effects of unravelling and can further enhance functional properties. These conjugates can find uses both as partial foods and as ingredients in the industry.</p>

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Enhancing the functional properties of hydrolyzed pea proteins using trypsin and Papain through Maillard conjugation with pea starch and other non-starch polysaccharides

  • 期刊论文

  • 发表日期：

    2025年6月5日

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  • Abhiroop Mookerjee,
  • Michael Nickerson,
  • Takuji Tanaka

摘要

Pea protein enriched flour was hydrolyzed using both proteases and amylases simultaneously, then it was heated to induce Maillard conjugation between proteins and polysaccharides. The resulting protein-starch conjugates were investigated for their structural, surface, and functional properties. SDS-polyacrylamide gel electrophoresis and scanning electron microscopy analyses showed the presence of different molecular species and altered microstructure in the conjugate preparations. The zeta potentials at pH 7 (− 20.6 to − 32.3 mV) and pH 10 (− 29.2 to − 36.6 mV) were more negative compared to pH 4 (0.2 to 8.6 mV), indicating higher exposure of ionized side chains. All trypsin-hydrolyzed protein-starch conjugates exhibited better foaming and emulsification properties compared to the papain-hydrolyzed protein-starch conjugates. Trypsin-hydrolyzed conjugates with a degree of hydrolysis (24%) showed the highest foam capacity (126.6%) at pH 7 and emulsion activity (24.0 m²/g) at pH 10. In contrast, trypsin hydrolysates (21.7% degree of hydrolysis) exhibited increased emulsion stability (99.4%) at pH 7. It is commonly considered that high degree of hydrolysis results in complete unraveling of proteins, leading to lower functionality. The results of this study showed that conjugation between proteins and polysaccharides can counterbalance the negative effects of unravelling and can further enhance functional properties. These conjugates can find uses both as partial foods and as ingredients in the industry.