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中国精品科技期刊2020
陆云峰,戴涛涛,李照莹,等. 高压射流协同pH循环处理对大米-豌豆复合蛋白功能性及结构的影响[J]. 食品工业科技,2025,46(2):1−11. doi: 10.13386/j.issn1002-0306.2024020218.
引用本文: 陆云峰,戴涛涛,李照莹,等. 高压射流协同pH循环处理对大米-豌豆复合蛋白功能性及结构的影响[J]. 食品工业科技,2025,46(2):1−11. doi: 10.13386/j.issn1002-0306.2024020218.
LU Yunfeng, DAI Taotao, LI Zhaoying, et al. Effects on the Functionality and Structure of Rice-pea Composite Protein by Industry-scale Microfluidizer Combined with pH Cycling Treatment[J]. Science and Technology of Food Industry, 2025, 46(2): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024020218.
Citation: LU Yunfeng, DAI Taotao, LI Zhaoying, et al. Effects on the Functionality and Structure of Rice-pea Composite Protein by Industry-scale Microfluidizer Combined with pH Cycling Treatment[J]. Science and Technology of Food Industry, 2025, 46(2): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024020218.

高压射流协同pH循环处理对大米-豌豆复合蛋白功能性及结构的影响

Effects on the Functionality and Structure of Rice-pea Composite Protein by Industry-scale Microfluidizer Combined with pH Cycling Treatment

  • 摘要: 为探究复合植物蛋白经高压射流磨与pH循环共同处理后的增溶作用,明晰其增溶机制,采用大米蛋白与豌豆蛋白作为原料,配制蛋白比例1:1,总蛋白浓度4%的混合蛋白溶液,并将混合液pH调整至12,在高压射流磨不同压力下进行处理,再将溶液pH调回中性后得到复合蛋白。采用氮溶解指数、粒径、荧光光谱、圆二色谱、分子量等手段表征本工艺过程中复合蛋白理化性质和结构的变化。结果表明,经高压射流磨协同pH循环处理4%的复合蛋白,复合蛋白氮溶解指数随着压力增大而提升,处理压力为120 MPa时,氮溶解指数为92.67%±0.77%。扫描电镜与粒径结果显示,射流磨处理后的复合蛋白尺寸降低,比表面积增大。内源荧光光谱、表面疏水性、巯基二硫键、圆二色谱结果显示,两种蛋白之间产生了相互作用,形成了新的共架体,且复合蛋白随处理压力增大,表面疏水性由4025.33显著增大至7359.45(P<0.05),疏水区域增加、游离巯基含量由26.46±0.32 μmol/g显著上升至最高32.66±0.35 μmol/g(P<0.05),二硫键含量由9.86±0.42 μmol/g显著下降至5.48±0.27 μmol/g(P<0.05),α-螺旋实际含量(25.3%)高于理论值(21.83%),二级结构向更亲水的α-螺旋转变。此外,氨基酸分析显示复合蛋白的氨基酸配比均衡完整。经处理后的复合蛋白在高溶解性的基础上,乳化与起泡性能均明显优于大米蛋白与豌豆蛋白。本研究表明高压射流磨协同pH循环的处理方法能够有效改善复合蛋白的功能特性,为植物蛋白工业化增溶改性提供理论支撑。

     

    Abstract: To investigate the solubilization of composite plant protein after co-processing with an industry-scale microfluidizer and pH cycling and to clarify its solubilization mechanism, this paper used rice protein and pea protein as raw materials, a mixed protein solution with a protein ratio of 1:1 and a total protein concentration of 4% were configured. The pH of the mixture was then adjusted to 12 and the solution processed at different pressures in a high-pressure jet mill. The composite protein was then obtained by adjusting the pH of the solution back to neutral. And to characterize the changes in physicochemical properties and structure of composite protein during this process using nitrogen solubility index, particle size, fluorescence spectroscopy, circular dichroism, molecular weight, and other means. Results showed that the nitrogen solubility index of 4% composite protein underwent industry-scale microfluidizer and pH cycling treatment was increased with the increase of pressure, reaching the maximum of 92.67%±0.77% at 120 MPa. The results of scanning electron microscopy and particle size showed that the composite proteins decreased in size and the specific surface area increased after the treatment of the industry-scale microfluidizer. The results of intrinsic fluorescence spectroscopy, surface hydrophobicity, sulfhydryl disulfide bonding, and circular dichroism indicated that the two proteins interacted to form new co-assembly composites. Surface hydrophobicity increased significantly from 4025.33 to 7359.45 (P<0.05), the hydrophobic region increased. Free sulfhydryl content increased significantly from 26.46±0.32 μmol/g to a maximum of 32.66±0.35 μmol/g (P<0.05), while disulphide bonding content decreased significantly from 9.86±0.42 μmol/g to 5.48±0.27 μmol/g (P<0.05). The actual content of α-helices (25.3%) was higher than the theoretical value (21.83%), indicating a transition to a more hydrophilic α-helix in the secondary structure as the treatment pressure increased. Furthermore, the amino acid analysis revealed that the composite protein had a balanced and complete composition of amino acids. Additionally, the emulsification and foaming properties of the treated composite proteins were superior to those of rice and pea proteins due to their high solubility. This study demonstrated that the combination of industry-scale microfluidizer and pH cycling can effectively enhance the functional properties of the composite protein. The findings provide theoretical support for solubilization and modification of plant proteins on an industrial scale.

     

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