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<p>The study investigated the effects of heat treatment and covalently bound galactose on the functional and structural properties of the jackfruit seed protein, clarifying their respective contributions during the glycation process. The protein-galactose conjugates (JGC) were prepared by wet-heating glycation at 90&#xa0;°C and compared with two control samples: the native, unheated jackfruit seed protein (JSPI<sub>N</sub>) and the heat-treated (90&#xa0;°C) jackfruit seed protein without galactose (JSPI<sub>H</sub>). The results indicated that heating has a greater effect on the functional properties of proteins, except for solubility, than covalently bound sugar molecules. Compared with JSPI<sub>N</sub>, the solubility, foam capacity, water holding capacity, and oil holding capacity of JSPI<sub>H</sub> and JGC increased by 43.98% and 106.74%, 280% and 320%, 110.6% and 136.4%, 24.4% and 48.1%, respectively. In addition, the denaturation temperatures of JSPI<sub>H</sub> and JGC were significantly increased to 98.61&#xa0;°C and 101.76&#xa0;°C. The relationship between the structure of the JGC and its solubility was further studied. From the analysis of the structure, covalent sugar binding altered the protein’s structural properties more significantly than heat treatment during the whole glycation process. Compared to JSPI<sub>N</sub>, the α-helix of JSPI<sub>H</sub> and JGC increased from 1.2 to 3.87% and 19.73%, respectively, while the β-sheet decreased from 32.7 to 33.83% and 20.53%, respectively, leading to the unfolding of protein molecules and depolymerization of the aggregates. The structural changes of JGC contributed to the exposure of the hydrophilic group and an increase in hydrophilicity after combining with galactose, resulting in enhanced solubility. In summary, heat treatment played a significant role in affecting the functional properties of the glycation process, whereas covalently bound sugar molecules had a major impact on the structural properties.</p>

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Influence of heat treatment and covalently bound galactose during glycation on the structural and physicochemical properties of jackfruit seed protein

  • 期刊论文

  • 发表日期：

    2026年2月17日

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  • Qingxue Ai,
  • Xiongfeng Zhang,
  • Wangruiqi Tang,
  • Yu Zhu,
  • Lei Zhou,
  • Wei Liu,
  • Chengmei Liu,
  • Fei Xu,
  • Yanjun Zhang,
  • Junzhen Zhong

摘要

The study investigated the effects of heat treatment and covalently bound galactose on the functional and structural properties of the jackfruit seed protein, clarifying their respective contributions during the glycation process. The protein-galactose conjugates (JGC) were prepared by wet-heating glycation at 90 °C and compared with two control samples: the native, unheated jackfruit seed protein (JSPIN) and the heat-treated (90 °C) jackfruit seed protein without galactose (JSPIH). The results indicated that heating has a greater effect on the functional properties of proteins, except for solubility, than covalently bound sugar molecules. Compared with JSPIN, the solubility, foam capacity, water holding capacity, and oil holding capacity of JSPIH and JGC increased by 43.98% and 106.74%, 280% and 320%, 110.6% and 136.4%, 24.4% and 48.1%, respectively. In addition, the denaturation temperatures of JSPIH and JGC were significantly increased to 98.61 °C and 101.76 °C. The relationship between the structure of the JGC and its solubility was further studied. From the analysis of the structure, covalent sugar binding altered the protein’s structural properties more significantly than heat treatment during the whole glycation process. Compared to JSPIN, the α-helix of JSPIH and JGC increased from 1.2 to 3.87% and 19.73%, respectively, while the β-sheet decreased from 32.7 to 33.83% and 20.53%, respectively, leading to the unfolding of protein molecules and depolymerization of the aggregates. The structural changes of JGC contributed to the exposure of the hydrophilic group and an increase in hydrophilicity after combining with galactose, resulting in enhanced solubility. In summary, heat treatment played a significant role in affecting the functional properties of the glycation process, whereas covalently bound sugar molecules had a major impact on the structural properties.