碱性pH偏移结合超声处理对花生蛋白结构与功能性质的影响

    Effect of alkaline pH shifting combined with ultrasound on the structural and functional properties of peanut protein

    • 摘要: 为了改善花生蛋白的功能性质,采用碱性pH偏移(pH 12和pH 13)单独或结合超声(500 W/5 min和30 min)处理花生蛋白,研究了处理前后花生蛋白结构、功能以及赖丙氨酸含量的变化情况。结果表明:所有处理方式均能提高花生蛋白的表面疏水性并使其内源荧光最大发射波长发生红移,其中pH 12偏移结合长时间超声处理、pH 13单独偏移或结合超声处理还能使花生蛋白可溶性聚集体含量显著增加,二级结构中α-螺旋含量减少、β-转角含量增加;pH 12或pH 13单独偏移均显著增加了花生蛋白中赖丙氨酸含量,而与超声结合处理后可使赖丙氨酸含量降低60%~66%;所有处理方式均能改善花生蛋白的溶解性和乳化性,其中pH 13偏移结合短时间超声处理使花生蛋白溶解度提高了23.23%,乳化活性和乳化稳定性指数分别增加了56%和271%,乳液的冻融稳定性显著增强。pH 13偏移结合超声处理不仅能显著提升花生蛋白的功能性质,而且可以有效抑制赖丙氨酸的产生,因此是一项应用潜力较高的蛋白复合改性技术。

       

      Abstract: To improve the functional properties of peanut protein, alkaline pH shift (pH 12 and pH 13) was used to treat peanut protein alone or combined with ultrasound (500 W/5 min and 30 min). The changes of in the structure, function, and lysalanine content of peanut protein before and after treatment were studied. The results showed that all treatment methods could increase the surface hydrophobicity of peanut protein and cause a red shift in the maximum emission wavelength of endogenous fluorescence. Among them, pH 12 shifting combined with long-term ultrasound treatment, pH 13 shifting alone, or combined with ultrasound treatment could also significantly increase the content of soluble aggregates in peanut protein, decrease α-helix and increase β-turn in the secondary structure. pH 12 or pH 13 shifting alone significantly increased the content of lysalanine in peanut protein, while the combination with ultrasonic treatment could reduce the content of lysalanine by 60%-66%. The solubility and emulsification of peanut protein were improved by pH 13 shifting combined with low-intensity ultrasound treatment, the solubility of peanut protein was increased by 23.23%, and the emulsifying activity and emulsifying stability index increased by 56% and 271%, respectively, and the freeze-thaw stability of the emulsion was significantly enhanced. pH 13 shifting combined with ultrasound treatment can not only significantly improve the functional properties of peanut protein, but also effectively inhibit the production of lysalanine. Therefore, it is a protein complex modification technology with high application potential.

       

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