食品科学 ›› 2023, Vol. 44 ›› Issue (6): 74-81.doi: 10.7506/spkx1002-6630-20220511-141

• 食品化学 • 上一篇    下一篇

动态高压微射流环境中豌豆白蛋白-绿原酸复合物的相互作用

嵇威,刘军,杨进洁,南希骏,厉佳怡,王红磊,盛桂华,周泉城   

  1. (1.山东理工大学农业工程与食品科学学院,山东 淄博 255049;2.山东禹王生态食业有限公司,山东 德州 251200;3.烟台双塔食品股份有限公司,山东 烟台 264000)
  • 出版日期:2023-03-27 发布日期:2023-03-27
  • 基金资助:
    山东省重点研发计划项目(2019GNC106084); 山东理工大学招远工业技术研究院创新研究基金项目(9101-219194;9101-220193);山东省研究生教育管理项目(117009)

Interaction of Pea Albumin with Chlorogenic Acid in a Dynamic High Pressure Microfluidization Environment

JI Wei, LIU Jun, YANG Jinjie, NAN Xijun, LI Jiayi, WANG Honglei, SHENG Guihua, ZHOU Quancheng   

  1. (1. College of Agricultural Engineering and Food Science, Shandong University of Technology, Zibo 255049, China; 2. Shandong Yuwang Ecological Food Industry Co. Ltd., Dezhou 251200, China; 3. Yantai Shuangta Food Co. Ltd., Yantai 264000, China)
  • Online:2023-03-27 Published:2023-03-27

摘要: 通过对豌豆白蛋白以及豌豆白蛋白-绿原酸复合物粒度、Zeta电位、荧光光谱、红外光谱与疏水性、溶解性、乳化特性等指标的测定,探究动态高压微射流不同处理压力对豌豆白蛋白和复合物结构与功能特性的影响,以及二元体系中绿原酸对豌豆白蛋白影响的机制和效果。结果表明,豌豆白蛋白经过动态高压微射流处理后,粒径与Zeta电位值均呈先降低后增加趋势;改性后的豌豆白蛋白微观结构、二级结构与三级结构均发生变化;剪切力等作用的小粒径豌豆白蛋白溶解性显著提高了42.37%,可达到0.84 mg/mL(P<0.05),乳化特性也得到一定增强。动态高压微射流处理加工豌豆白蛋白-绿原酸复合物体系中,绿原酸改变了豌豆白蛋白色氨酸的微环境,使白蛋白结构发生显著变化。绿原酸使豌豆白蛋白表面疏水性显著增加(P<0.05),溶解性显著降低(P<0.05),并将豌豆白蛋白乳化活性提高。本研究阐释了动态高压微射流和绿原酸对豌豆白蛋白的影响作用,为豌豆白蛋白改性提供思路,为高值化蛋白产品的开发提供一定理论基础。

关键词: 动态高压微射流;豌豆白蛋白;绿原酸;物理改性

Abstract: In this study, the effect of dynamic high pressure microfluidization at different pressures on the structural and functional properties of pea albumin and its complex with chlorogenic acid was investigated by measuring particle size, zeta potential, fluorescence spectra, infrared spectra, hydrophobicity, solubility and emulsification properties. The mechanism of the influence of chlorogenic acid on pea albumin in the binary system was explored. The results showed that after dynamic high pressure microfluidization treatment, the particle size and zeta potential of pea albumin firstly decreased and then increased. The microstructure, secondary structure and tertiary structure of pea albumin were changed. The solubility of small pea albumin particles was significantly increased by 42.37%, reaching 0.84 mg/mL under the action of shear force and other effects (P < 0.05), and the emulsification characteristics were also enhanced. The addition of chlorogenic acid changed the microenvironment of tryptophan residues in pea albumin, which led to significant changes in the structure of pea albumin. Meanwhile, it significantly increased the surface hydrophobicity and decreased the solubility of pea albumin (P < 0.05), and improved the solubility. This study provides an idea for pea albumin modification and a theoretical foundation for the development of high-value protein products.

Key words: dynamic high pressure microfluidization; pea albumin; chlorogenic acid; physical modification

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