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<p>Germination is an eco-friendly green technology that improves nutritional and techno-functional quality of plant-based proteins. This study examined the functional, structural, thermal, and in vitro digestibility of protein isolates from germinated mung beans at 0–120&#xa0;h. A significant effect was seen in the protein content of mung bean protein isolate after 120&#xa0;h, which increased from 6.18 to 9.87%. The structural modification of mung bean protein isolate (MBPI) induced by germination increased solubility, water binding capacity, emulsion capacity, and foaming capacity by 48.35%, 155.21%, 27.08% and 113.97% respectively. The in vitro protein digestibility and antioxidant activity of mung bean protein were also increased after germination. The results showed a marked increase in surface hydrophobicity and sulfhydryl content following germination. This was confirmed through multispectral analysis, including SEM and FTIR, which indicated that germinated MBPI underwent a structural transition, leading to an exposed and unfolded structure. Furthermore, analysis of the amide I secondary structure revealed a decrease in β-sheets (from 41.37% to 30.68%) and β-turns (from 28.15% to 20.86%), alongside an increase in α-helix (from 17.47% to 29.35%) and random coils (from 13.01% to 19.11%) in MBPI after 120&#xa0;h of germination. The results indicated that germination treatment may increase the structural and functional features of mung bean proteins which could be a great way to improve the nutritional qualities and processing value of plant seed proteins.</p>

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Germination-driven enhancements in structural, functional properties, and in vitro digestibility of mung bean protein isolate

  • 期刊论文

  • 发表日期：

    2025年11月7日

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  • Manasi Ajit More,
  • Priya Negi,
  • Rhythm Kalsi,
  • Jasleen Kaur,
  • Piyush Kashyap

摘要

Germination is an eco-friendly green technology that improves nutritional and techno-functional quality of plant-based proteins. This study examined the functional, structural, thermal, and in vitro digestibility of protein isolates from germinated mung beans at 0–120 h. A significant effect was seen in the protein content of mung bean protein isolate after 120 h, which increased from 6.18 to 9.87%. The structural modification of mung bean protein isolate (MBPI) induced by germination increased solubility, water binding capacity, emulsion capacity, and foaming capacity by 48.35%, 155.21%, 27.08% and 113.97% respectively. The in vitro protein digestibility and antioxidant activity of mung bean protein were also increased after germination. The results showed a marked increase in surface hydrophobicity and sulfhydryl content following germination. This was confirmed through multispectral analysis, including SEM and FTIR, which indicated that germinated MBPI underwent a structural transition, leading to an exposed and unfolded structure. Furthermore, analysis of the amide I secondary structure revealed a decrease in β-sheets (from 41.37% to 30.68%) and β-turns (from 28.15% to 20.86%), alongside an increase in α-helix (from 17.47% to 29.35%) and random coils (from 13.01% to 19.11%) in MBPI after 120 h of germination. The results indicated that germination treatment may increase the structural and functional features of mung bean proteins which could be a great way to improve the nutritional qualities and processing value of plant seed proteins.