大豆蛋白热聚集行为控制及其结构表征的研究
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摘要
热处理是大豆蛋白加工中常用的手段。热诱导下的蛋白质聚集行为对产品的结构及功能有着决定性的影响。本论文研究了大豆蛋白主要组分β-伴大豆球蛋白（β-conglycinin，7S）和大豆球蛋白（glycinin，11S）在热处理过程中的聚集行为，对加热过程中所形成聚集体的结构进行了表征，阐述了大豆蛋白溶解性与聚集行为之间的关系，并利用其聚集行为通过控制各种环境因素制备了可用于食品加工的大豆蛋白聚集体颗粒。主要研究结果如下：
1）运用小角度X-射线散射（SAXS）和分子排阻色谱-小角度静态光散射联用（SEC-LALS）技术对大豆7S和11S蛋白质的热聚集行为进行研究，并对两者所形成的可溶性及不溶性聚集体的绝对分子量、蛋白质颗粒的形状和结构进行表征，揭示了两种聚集体结构的差异与其溶解性的关系。通过Lumry-Eyring成核聚合（LENP）模型对7S和11S的热聚集动力学进行比较，首次发现了7S的热聚集是有限聚集，7S以单体添加的方式形成结构相对松散的可溶性聚集体；11S的热聚集行为与7S不同，其聚集程度较7S高，聚集体间的凝聚作用是11S聚集体形成的主要驱动力，粒径的大幅增加以及聚集体内密度分布的改变使该聚集体成为不溶性聚集体；7S在加热过程中与11S形成复合物，限制了11S的聚集程度，使11S的聚集终止在聚合阶段，从而大幅减少11S由热处理所引起的溶解性损失。疏水作用是加热过程中7S-11S复合物形成的主要驱动力。
2）以“人工分子伴侣”SDS和大豆11S进行模型试验，对“人工分子伴侣”抑制大豆蛋白热聚集的机制进行研究。结果表明，具有双亲性结构的SDS与11S在中性pH条件下通过彼此疏水基团的相互作用形成复合物。11S分子表面的疏水基团被屏蔽，SDS的亲水基团为11S分子带来强大的静电屏障，阻止了11S分子的相互靠近，从而抑制了11S的热聚集。大豆蛋白的热聚集是由分子间的疏水作用与静电斥力的相互关系决定的。屏蔽暴露的疏水基团、同时引入亲水或带电的基团是抑制大豆蛋白聚集、提高其溶解性的有效策略。
3）研究了单独的物理处理对大豆蛋白溶解性的影响，发现了水热处理可大幅提高11S碱性多肽的溶解性。结果表明，在碱性条件下，提高体系的pH值、增加水热处理的压力、延长处理时间、降低体系内的蛋白质含量及离子强度均有利于提高水热处理的增溶作用。对该作用的机理研究发现，不溶性聚集体的结构在高温高压的条件下得以展开。当温度和压力的条件消失后，展开的蛋白质分子在环境因素以及自身性质的诱导下进行分子重排（rearrange）。对环境因素进行控制，降低蛋白质在此条件下的重聚集程度便可提高水热处理的增溶作用。
4）通过在接近11S等电点的pH范围对其进行热处理制备了大豆11S蛋白质聚集体颗粒。结果显示，该聚集体颗粒的平均粒径为157nm，粒径PdI为0.105，该法制备聚集体颗粒的得率约为80％。疏水作用和氢键是形成该聚集体颗粒的主要驱动力。该聚集体颗粒经过干燥、重新悬浮后，在多个pH条件下仍具有良好的分散性及热稳定性。此外，该聚集体颗粒具有弱化蛋白质凝胶的作用。
5）通过对大豆蛋白凝胶进行高压均质分散制备了大豆蛋白聚集体颗粒。结果表明，该蛋白质聚集体颗粒的粒径及稳定性主要取决于均质pH值和离子强度。当以远离大豆蛋白等电点的pH条件进行均质，可获得稳定、均匀分散于水相体系中的蛋白质聚集体颗粒。该颗粒包埋转谷氨酰胺酶（Microbial transglutaminase，MTGase）后可诱导变性大豆分离蛋白（soy protein isolates，SPI）交联形成凝胶。表明该颗粒可对活性物质进行包埋及释放，可作为功能成分输送载体应用于食品加工中。
Heat treatment is commonly used in soy protein processing. The structural and functionalproperties of the products are determined by the thermal aggregation behavior of soy protein.In this work, the thermal aggregation behaviors of β-conglycinin (7S) and glycinin (11S) themain fractions in soy protein were studied, the structure of the aggregates formed duringheating was characterized, the relation between protein solubility and protein aggregation wasdiscussed, and the soy protein aggregate particles which were able to carry bio-activemolecules were prepared. Main results are as follows:
1) The thermal aggregation kinetics of soybean7S and11S were studied with size exclusionchromatography and low-angle light scattering (SEC-LALS), and the structure of the solubleand insoluble aggregates was analyzed by small-angle X-ray scattering (SAXS). TheLumry-Eyring nucleated polymerization (LENP) was used to elucidate the thermalaggregation behaviors of7S and11S. It was found that7S and11S possessed differentthermal aggregation behaviors. With limited aggregation,7S soluble aggregates had lesscompact structure grew via monomer addition. On the contrary, the aggregation of11S wasnot restricted. Condensation between the aggregates occurred in the thermal aggregation of11S. Significant increase of the particle size and density in the core turned the11S aggregatesinto insoluble materials.7S-11S complex was formed, when11S was heated with7S. In thiscase, the aggregation of11S was restricted and terminated at the polymerization stage in thepresence of7S. As a result, the solubility loss of11S caused by heating was recovered. Andhydrophobic interaction played an important role in the preferential interaction between7Sand11S.
2) In order to reveal the mechanism that the thermal aggregation of soy protein could besuppress by artificial molecular chaperone, SDS and soybean11S were used to perform themodel test. It was found that SDS-11S complex was formed under the interaction between thehydrophobic groups on these two molecules at neutral pH. The exposed hydrophobic groupson the surface of11S were covered, and plenty of charged groups which could produce strongelectrostatic barriers were brought to the surface of11S. As a result, the11S particles werehard to approach to each other and the thermal aggregation could not occur. The aggregation tendency of protein was determined by the competition between the hydrophobic attractionand electrostatic repulsion. Shielding the exposed hydrophobic residues and employing morehydrophilic groups on the surface of the protein molecules is an effective strategy forimproving the solubility of soy protein during processing.
3) The effect of physical treatment on the solubility of soy protein was studied. It was foundthat the solubility of basic polypeptides was greatly improved by hydrothermal cooking(HTC). It was suggested that higher pH of the dispersion, stronger steam pressure, longertreated time, less protein content and ionic strength of the dispersion were favorable forincreasing the solubility of basic polypeptides after HTC with alkaline conditions. Thestructure of insoluble aggregates unfolded under the effect of high temperature and high steampressure. As this effect was removed, the protein molecules rearranged under the guidance ofits primary structure and the surrounding conditions. Proper environment conditions were ableto decrease the reaggregation extent of these protein molecules and improve the solubilizationeffect of HTC.
4) The soybean11S aggregate particles were prepared by heating11S dispersion at pH nearits pI. The mean particle size of these particles was157nm, and the particle size PdI was0.105. The yield of these particles was about80%. Hydrophobic interaction and hydrogenbonds were the main driving force for the formation of the11S aggregate particles. After driedand redispered, the particles maintained good dispersiveness and thermal stability underseveral pH conditions. In addition, these11S aggregate particles could weaken theprotein-based gel network.
5) The soy protein aggregate particles were prepared by homogenizing the soy protein gelinduced by gluconic acid-δ-lactone (GDL). The particle size and colloidal stability weredetermined by the pH and ionic strength of the dispersion during homogenizing. Stabledispersed particles appeared when homogenizing was conducted at pH far from the pI of soyprotein. Microbial transglutaminase (MTGase) was entrapped in these particles. Whendispersed in the denatured soy protein isolates (SPI) dispersions, gels were formed with theseMTGase entrapped particles. It suggested that these particles could be used as a bio-activemolecule carrier in food processing.
1）运用小角度X-射线散射（SAXS）和分子排阻色谱-小角度静态光散射联用（SEC-LALS）技术对大豆7S和11S蛋白质的热聚集行为进行研究，并对两者所形成的可溶性及不溶性聚集体的绝对分子量、蛋白质颗粒的形状和结构进行表征，揭示了两种聚集体结构的差异与其溶解性的关系。通过Lumry-Eyring成核聚合（LENP）模型对7S和11S的热聚集动力学进行比较，首次发现了7S的热聚集是有限聚集，7S以单体添加的方式形成结构相对松散的可溶性聚集体；11S的热聚集行为与7S不同，其聚集程度较7S高，聚集体间的凝聚作用是11S聚集体形成的主要驱动力，粒径的大幅增加以及聚集体内密度分布的改变使该聚集体成为不溶性聚集体；7S在加热过程中与11S形成复合物，限制了11S的聚集程度，使11S的聚集终止在聚合阶段，从而大幅减少11S由热处理所引起的溶解性损失。疏水作用是加热过程中7S-11S复合物形成的主要驱动力。
2）以“人工分子伴侣”SDS和大豆11S进行模型试验，对“人工分子伴侣”抑制大豆蛋白热聚集的机制进行研究。结果表明，具有双亲性结构的SDS与11S在中性pH条件下通过彼此疏水基团的相互作用形成复合物。11S分子表面的疏水基团被屏蔽，SDS的亲水基团为11S分子带来强大的静电屏障，阻止了11S分子的相互靠近，从而抑制了11S的热聚集。大豆蛋白的热聚集是由分子间的疏水作用与静电斥力的相互关系决定的。屏蔽暴露的疏水基团、同时引入亲水或带电的基团是抑制大豆蛋白聚集、提高其溶解性的有效策略。
3）研究了单独的物理处理对大豆蛋白溶解性的影响，发现了水热处理可大幅提高11S碱性多肽的溶解性。结果表明，在碱性条件下，提高体系的pH值、增加水热处理的压力、延长处理时间、降低体系内的蛋白质含量及离子强度均有利于提高水热处理的增溶作用。对该作用的机理研究发现，不溶性聚集体的结构在高温高压的条件下得以展开。当温度和压力的条件消失后，展开的蛋白质分子在环境因素以及自身性质的诱导下进行分子重排（rearrange）。对环境因素进行控制，降低蛋白质在此条件下的重聚集程度便可提高水热处理的增溶作用。
4）通过在接近11S等电点的pH范围对其进行热处理制备了大豆11S蛋白质聚集体颗粒。结果显示，该聚集体颗粒的平均粒径为157nm，粒径PdI为0.105，该法制备聚集体颗粒的得率约为80％。疏水作用和氢键是形成该聚集体颗粒的主要驱动力。该聚集体颗粒经过干燥、重新悬浮后，在多个pH条件下仍具有良好的分散性及热稳定性。此外，该聚集体颗粒具有弱化蛋白质凝胶的作用。
5）通过对大豆蛋白凝胶进行高压均质分散制备了大豆蛋白聚集体颗粒。结果表明，该蛋白质聚集体颗粒的粒径及稳定性主要取决于均质pH值和离子强度。当以远离大豆蛋白等电点的pH条件进行均质，可获得稳定、均匀分散于水相体系中的蛋白质聚集体颗粒。该颗粒包埋转谷氨酰胺酶（Microbial transglutaminase，MTGase）后可诱导变性大豆分离蛋白（soy protein isolates，SPI）交联形成凝胶。表明该颗粒可对活性物质进行包埋及释放，可作为功能成分输送载体应用于食品加工中。
Heat treatment is commonly used in soy protein processing. The structural and functionalproperties of the products are determined by the thermal aggregation behavior of soy protein.In this work, the thermal aggregation behaviors of β-conglycinin (7S) and glycinin (11S) themain fractions in soy protein were studied, the structure of the aggregates formed duringheating was characterized, the relation between protein solubility and protein aggregation wasdiscussed, and the soy protein aggregate particles which were able to carry bio-activemolecules were prepared. Main results are as follows:
1) The thermal aggregation kinetics of soybean7S and11S were studied with size exclusionchromatography and low-angle light scattering (SEC-LALS), and the structure of the solubleand insoluble aggregates was analyzed by small-angle X-ray scattering (SAXS). TheLumry-Eyring nucleated polymerization (LENP) was used to elucidate the thermalaggregation behaviors of7S and11S. It was found that7S and11S possessed differentthermal aggregation behaviors. With limited aggregation,7S soluble aggregates had lesscompact structure grew via monomer addition. On the contrary, the aggregation of11S wasnot restricted. Condensation between the aggregates occurred in the thermal aggregation of11S. Significant increase of the particle size and density in the core turned the11S aggregatesinto insoluble materials.7S-11S complex was formed, when11S was heated with7S. In thiscase, the aggregation of11S was restricted and terminated at the polymerization stage in thepresence of7S. As a result, the solubility loss of11S caused by heating was recovered. Andhydrophobic interaction played an important role in the preferential interaction between7Sand11S.
2) In order to reveal the mechanism that the thermal aggregation of soy protein could besuppress by artificial molecular chaperone, SDS and soybean11S were used to perform themodel test. It was found that SDS-11S complex was formed under the interaction between thehydrophobic groups on these two molecules at neutral pH. The exposed hydrophobic groupson the surface of11S were covered, and plenty of charged groups which could produce strongelectrostatic barriers were brought to the surface of11S. As a result, the11S particles werehard to approach to each other and the thermal aggregation could not occur. The aggregation tendency of protein was determined by the competition between the hydrophobic attractionand electrostatic repulsion. Shielding the exposed hydrophobic residues and employing morehydrophilic groups on the surface of the protein molecules is an effective strategy forimproving the solubility of soy protein during processing.
3) The effect of physical treatment on the solubility of soy protein was studied. It was foundthat the solubility of basic polypeptides was greatly improved by hydrothermal cooking(HTC). It was suggested that higher pH of the dispersion, stronger steam pressure, longertreated time, less protein content and ionic strength of the dispersion were favorable forincreasing the solubility of basic polypeptides after HTC with alkaline conditions. Thestructure of insoluble aggregates unfolded under the effect of high temperature and high steampressure. As this effect was removed, the protein molecules rearranged under the guidance ofits primary structure and the surrounding conditions. Proper environment conditions were ableto decrease the reaggregation extent of these protein molecules and improve the solubilizationeffect of HTC.
4) The soybean11S aggregate particles were prepared by heating11S dispersion at pH nearits pI. The mean particle size of these particles was157nm, and the particle size PdI was0.105. The yield of these particles was about80%. Hydrophobic interaction and hydrogenbonds were the main driving force for the formation of the11S aggregate particles. After driedand redispered, the particles maintained good dispersiveness and thermal stability underseveral pH conditions. In addition, these11S aggregate particles could weaken theprotein-based gel network.
5) The soy protein aggregate particles were prepared by homogenizing the soy protein gelinduced by gluconic acid-δ-lactone (GDL). The particle size and colloidal stability weredetermined by the pH and ionic strength of the dispersion during homogenizing. Stabledispersed particles appeared when homogenizing was conducted at pH far from the pI of soyprotein. Microbial transglutaminase (MTGase) was entrapped in these particles. Whendispersed in the denatured soy protein isolates (SPI) dispersions, gels were formed with theseMTGase entrapped particles. It suggested that these particles could be used as a bio-activemolecule carrier in food processing.
引文
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