大豆蛋白的结构表征及应用研究
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摘要
大豆因具有极高的营养价值和优良的保健功能在食品工业中大放异彩,同时由于大豆中含有高达40%的蛋白质,因此促使科学家们不断探索,期望从了解天然蛋白质材料的结构与性能之间的关系入手,借鉴自然界的力量开发出具有优异性能的大豆蛋白材料。大豆蛋白主要组分是7S球蛋白和11S球蛋白,两者占到蛋白质总含量的87%,基本代表了纯大豆蛋白的营养价值、物化性能以及生理功能等。对大豆蛋白进行仔细而深入的基础研究,有利于弄清其结构和性能之间的关系,从而能够有的放矢地设计和制备各类基于大豆蛋白的天然材料,充分发挥大豆蛋白全天然、可再生、可回收等绿色环保的特点。
大豆蛋白具有复杂的组成和结构,亚基内和亚基间存在较强的相互作用,形成紧密的聚集态结构,不利于其在水中溶解,因此,制备均匀、稳定的大豆蛋白水溶液对于后续研究非常重要。我们采用了两种常见的生化试剂——盐酸胍和二硫苏糖醇(或巯基乙醇)来破坏大豆蛋白中的氢键和二硫键,再经过透析将它们除去,从而获得浓度为3.0 wt%左右,并且分子链未发生明显降解的大豆蛋白水溶液。将3.0 wt%的大豆蛋白水溶液进一步采用聚乙二醇水溶液进行反向透析后可获得浓度更高的大豆蛋白水溶液用于后续研究。大豆蛋白溶液性质对于我们充分理解并改善大豆蛋白材料结构和性能至关重要,因此我们接着采用流变技术考察了大豆蛋白溶液性质。研究结果发现大豆蛋白溶液的浓度是其流变性质的重要影响因素。当大豆蛋白溶液浓度小于等于7.2 wt%时其在低频区的模量几乎不随浓度而变化且弹性模量大于损耗模量,说明溶液中存在某种微凝胶结构；当溶液浓度大于等于9.0 wt%时,大豆蛋白溶液的流变性质发生显著变化,其动态模量与频率有如下关系：G′(ω)～G″(ω)～ω″,且损耗角tanδ与频率ω无关,符合Winter的自相似松驰模型,即当浓度等于临界浓度113 wt%时，储存模量与损耗模量相等,形成亚稳定临界凝胶；低于11.3 wt%时转变为溶液状态而高于11.3wt%时会形成弱凝胶。
大豆蛋白构象及其聚集态结构与其功能有着密切的关系,本论文详细讨论了热诱导大豆蛋白膜的构象转变过程,并提出其构象转变机理。在升温过程中,外界热能使得大豆蛋白膜中蛋白质分子链及链段运动得以实现,发生局部调整或重排,部分不稳定的无规线团构象遭到破坏,形成了较为稳定的β-转角构象。通过对特征峰随温度升高的变化曲线图以及二维相关红外光谱分析,我们将1500cm-1处的特征峰归属于与1700 cm-1处同源的p-转角构象。同时我们发现酰胺Ⅰ的变化速率要快于1550 cm-1处特征峰的变化速率,究其原因我们认为该处吸收峰是酰胺Ⅱ和酪氨酸残基振动的协调效果。大豆蛋白膜在一定温度下随时间的增加而发生的构象转变机理在本质上与通过加热诱导的构象转变机理相同。升降温循环实验则表明了热诱导大豆蛋白膜的大豆蛋白大约有30%～40%的构象具有可逆回复的性质,但是,1700 cm-1处的特征峰在降温再升温过程中几乎没有变化,表明大豆蛋白通过热诱导形成的p-转角构象比较稳定。
蛋白质材料通常在制备后很短时间内(几个小时或者更短的时间)会发生结构的变化,如较容易吸收空气中的水分使其力学性能发生改变,为日后的使用带来很大的不便。因此我们在通过红外光谱考察大豆蛋白膜热诱导其构象转变的基础上,结合热力学分析(TGA和DMTA)从分子水平上来重点讨论水在大豆蛋白膜构象转变中的作用。结合这三种不同的测试方法进行动力学分析,我们发现大豆蛋白膜的构象转变速率与蛋白质热力学次级松弛过程中的其分子链氨基酸残基上缔合的水分子经升温后的脱离过程有密切联系。在加热过程中,随着水分子活动能力的增加,蛋白质主链上氨基酸残基的氢键被破坏,取而代之的是脱离水分子后的氨基酸残基间形成了新的氢键,从而引起蛋白质分子链的构象转变。但是我们的研究表明,简单的水蒸发过程并不能提供足够的活化能使蛋白质分子链发生重排,而是蛋白质变性或其玻璃化转变过程中水与氨酸残基之间相互作用引起的弹性不稳定状态导致了其从无序结构向有序结构转变。
在研究大豆蛋白构象转变机理的同时,制备纯天然大豆蛋白材料是本论文的另一研究目的。虽然大豆蛋白在膜材料、纤维和塑料领域有一定的应用,但是将其作为智能型水凝胶方面的应用却未见报道。由于大豆蛋白的分子链上含有较多的酸性和碱性氨基酸残基,具有相当数量的可离子化基团,因此,我们成功将其制备成了一种具有较好力学性能的电场敏感水凝胶。作为一种蛋白质水凝胶,大豆蛋白水凝胶上所带电荷的种类和数量取决于电解质溶液的pH值及其本身的等电点。当pH值接近大豆蛋白质等电点时,大豆蛋白凝胶上所带的电荷数量非常少,因此在pH=6的电解质溶液中大豆蛋白水凝胶几乎没有电场响应性。在pH<6的缓冲溶液中,大豆蛋白水凝胶具有聚阳离子的性质,在电场的作用下弯向阳极；在pH>6的缓冲溶液中,该水凝胶变为聚阴离子,在电场的作用下弯向阴极。在pH=2-4和pH=10-12范围内,水凝胶的平衡弯曲角可以达到60°以上,甚至在pH=2以及pH=12时,电压为20 V的条件下可以达到90°。另外,在pH=7的中性条件下,大豆蛋白水凝胶弯向阴极,电压为20 V时平衡弯曲角度可以达到21°。这些结果表明了我们制备的大豆蛋白水凝胶是一种性能良好的天然高分子电场敏感水凝胶,在很宽的pH值范围均具有较好的电场响应性,优于我们课题组先前报道的壳聚糖/羧甲基纤维素水凝胶和壳聚糖/羧甲基壳聚糖水凝胶。除溶液的pH值外,电压的大小、溶液的离子强度等都会影响大豆蛋白水凝胶的电场响应性,并且大豆蛋白水凝胶的弯曲行为具有很好的重复性,这些特点表明该水凝胶在微型传感器、微型驱动器以及人工肌肉方面具有潜在的应用价值。此外,在环形电场刺激下,大豆蛋白水凝胶环也有很好的刺激响应性,拓展了其应用范围,为日后大豆蛋白电场敏感水凝胶的实际应用奠定了基础。
综上所述,我们首先获得了分子链未降解的高浓度大豆蛋白溶液,然后采用流变技术测定了其溶液性质,用红外光谱研究了其构象转变,同时结合热力学分析,提出了大豆蛋白在热诱导下的构象转变机理。最后我们成功制备了一种具有相当应用潜力的大豆蛋白电场敏感水凝胶,并详细研究了影响其电场响应性的因素。由此,本论文分别从基础研究和实际应用两方面对大豆蛋白这一种天然高分子材料进行了较为系统的研究,期望能够加深对大豆蛋白这种来源丰富,可资源再生的天然高分子材料的了解,拓展其应用领域。
Soybean has a long history in the food industry owing to its high nutritional value and processability. However, soybean also contains a large fraction of proteins (up to 40%) that has attracted research interests for the development of environment-friendly protein materials with potential excellent physical properties. Soy protein isolate (SPI), more than 90% protein content, contains two major components:glycinin (11S, approximately 52% of the total protein content) and (3-conglycinin (7S, approximately 35% of the total protein content). These two components are responsible for the nutritional, physicochemical and physiological properties of soy proteins. In order to take full advantage of the green feature of soy protein, a fundamental understanding of the relationship between structure and properties of soy protein will be very valuable for the preparation and application of natural protein materials in the future, as well as the more direct application to soy-based foodstuffs and environmentally friendly structural polymers.
Soy protein has complex composition and structure and there are relatively strong interactions in and between the subunits, which prevents soy protein from dissolving in water. Therefore, the preparation of uniform and steady aqueous solution of soy protein is important for further investigation. Herein, two biochemical agents, guandine hydrocholoride (GuIICl) and dithiothreitol (DTT), were used to destroy the hydrogen bonds and disulfide bonds in soy protein, which were removed by dialysis against water to obtain soy protein solution with initial concentration of 3.0 wt% and without obvious degradation. More concentrated soy protein solutions were obtained by reverse dialysis against PEG solution. It is essential to know the properties of soy protein solution for fully understanding and improving the structure and properties of soy protein. So rheological measurements were applied to study the properties of soy protein solution with different concentrations. When the concentration was equal to or lesser than 7.2 wt%, the modulus were independent on the concentrations of soy protein solution and the storage modulus were higher than the loss modulus in low frequency, observations revealed the existence of some microgel structure. However, there was a significant change when the concentration was equal to or higher than 9.0 wt%, the dynamic modulus and the frequency conformed to the following relations:G′(ω)～G″(ω)～ωn, fitting in with Winter's self-similar relaxation line model, that is, when the concentration is equar to the critical concentration 11.3 wt% it can form an metastable critical gel; otherwise, when the concentration is lower than 11.3 wt% it changed to solution while weak gel could form when the concentration is higher than 11.3 wt%.
The functions of soy protein are closely related to its conformation and aggregation structure, so the thermally-induced conformational transitions of soy protein films were studied detailedly and corresponding mechanism of conformational changes was proposed. In the heating process, the heat energy made the soy protein molecular chain segment move with partial adjustment or rearrangement, some volatile random coil structure destructed and formed a relatively stable P-turn conformation. We also suggested that the peak at 1500 cm-1 was assigned to the characteristic of p-turn with the homologous at the peak of 1700 cm-1 according to FTIR and 2D-IR. The rate of change in amide I was faster than at the peak of 1550 cm-1 because of the combination mode of amide II and Tyrosine. The mechanism of conformational transitions of soybean protein films under isothermal conditions was the same as in the heating process. Moreover, the observations in heated-cooled-heated experiment revealed that about 30%～40 %conformation could be reversible, however, the peak at 1700 cm-1 had little change which showed that the heating-inducedβ-turn conformation was very stable.
Generally speaking, properties such as water pick-up and mechanical properties of protein materials are often seen to change significantly over a period of minutes or hours after preparation, even under moderate laboratory conditions around ambient temperature. So we tried to study the effect of water on the thermally-induced conformational transitions of soy protein films. By comparing the kinetics of protein-water interactions as a function of temperature using time resolved FTIR, TGA, and DTMA measurements on soybean protein films, we found that simply evaporating water from the film (TGA) is insufficient to explain the rate of conformational changes (FTIR and DMTA). The onset of mobility in the water molecules allows the amide groups to reconfigure and form stronger amide-amide hydrogen bonds. Thus, simple loss of water (evaporation) is insufficient by itself to allow the protein chains to reconfigure, which requires an activation step for the water to become mobile. We suggest that an elastic instability condition of denaturation or glass transition events in water-amide interactions is the governing mechanism for conformational changes that allows the evolution of disordered structures into more ordered secondary structures, thereby controlling the changes in physical properties such as stiffness and water sensitivity.
Owing to its sustainability, abundance, low cost and functionality, soy protein has attracted great research interests for the development of environment-friendly protein materials with potentially good properties, such as regeneration, biocompatibility and biodegradability, etc. To date, numerous soy protein-based materials have been studied which can be divided into plastics, gels, films, and additives or coatings. However, there have not been any studies on electroactive protein hydrogels made of pristine soy protein. A natural electroactive protein hydrogel was prepared from soy protein isolate (SPI) solution by crosslinking with epichlorohydrin. Under electrical stimulus, such SPI hydrogel quickly bends towards one electrode, showing a good electroactivity. Because of its amphoteric nature, the SPI hydrogel bends either toward the anode (pH< 6) or cathode (pH> 6), depending on the pH of the electrolyte solution. Other factors, such as electric field strength and ionic strength also influence the electromechanical behavior of the SPI hydrogels. Moreover, this SPI hydrogel exhibits a good electroactive behavior under strong acidic (pH=2-4) or basic (pH=10-12) solutions, which is a significant improvement over two other kinds of natural electroactive hydrogels, i.e., chitosan/carboxymethylcellulose and chitosan/carboxymethylchitosan hydrogel, which we reported previously. The wide pH range and good electroactivity of this natural protein hydrogel suggests its great potential for microsensor and actuator applications, especially in the biomedical field, and also to increase the scope of natural polymer-based electroactive hydrogels.
In conclusion, we first obtained high concentrated soy protein solution without obvious degradation and also studied the properties of this solution by rheological measurements. Then, we studied the thermally-induced conformational transitions of soy protein films detailedly by FTIR and thermodynamic analysis and suggested the mechanism of conformational changes. At last, we successfully prepared a natural electroactive protein hydrogel from soy protein solution by crosslinking with epichlorohydrin. Thus, in this thesis, we systematically studied the soy protein in both the basic research and its practical application, so as to learn more about the soy protein from the perspective of bipolymer and finally expand its applications.
大豆蛋白具有复杂的组成和结构,亚基内和亚基间存在较强的相互作用,形成紧密的聚集态结构,不利于其在水中溶解,因此,制备均匀、稳定的大豆蛋白水溶液对于后续研究非常重要。我们采用了两种常见的生化试剂——盐酸胍和二硫苏糖醇(或巯基乙醇)来破坏大豆蛋白中的氢键和二硫键,再经过透析将它们除去,从而获得浓度为3.0 wt%左右,并且分子链未发生明显降解的大豆蛋白水溶液。将3.0 wt%的大豆蛋白水溶液进一步采用聚乙二醇水溶液进行反向透析后可获得浓度更高的大豆蛋白水溶液用于后续研究。大豆蛋白溶液性质对于我们充分理解并改善大豆蛋白材料结构和性能至关重要,因此我们接着采用流变技术考察了大豆蛋白溶液性质。研究结果发现大豆蛋白溶液的浓度是其流变性质的重要影响因素。当大豆蛋白溶液浓度小于等于7.2 wt%时其在低频区的模量几乎不随浓度而变化且弹性模量大于损耗模量,说明溶液中存在某种微凝胶结构；当溶液浓度大于等于9.0 wt%时,大豆蛋白溶液的流变性质发生显著变化,其动态模量与频率有如下关系：G′(ω)～G″(ω)～ω″,且损耗角tanδ与频率ω无关,符合Winter的自相似松驰模型,即当浓度等于临界浓度113 wt%时，储存模量与损耗模量相等,形成亚稳定临界凝胶；低于11.3 wt%时转变为溶液状态而高于11.3wt%时会形成弱凝胶。
大豆蛋白构象及其聚集态结构与其功能有着密切的关系,本论文详细讨论了热诱导大豆蛋白膜的构象转变过程,并提出其构象转变机理。在升温过程中,外界热能使得大豆蛋白膜中蛋白质分子链及链段运动得以实现,发生局部调整或重排,部分不稳定的无规线团构象遭到破坏,形成了较为稳定的β-转角构象。通过对特征峰随温度升高的变化曲线图以及二维相关红外光谱分析,我们将1500cm-1处的特征峰归属于与1700 cm-1处同源的p-转角构象。同时我们发现酰胺Ⅰ的变化速率要快于1550 cm-1处特征峰的变化速率,究其原因我们认为该处吸收峰是酰胺Ⅱ和酪氨酸残基振动的协调效果。大豆蛋白膜在一定温度下随时间的增加而发生的构象转变机理在本质上与通过加热诱导的构象转变机理相同。升降温循环实验则表明了热诱导大豆蛋白膜的大豆蛋白大约有30%～40%的构象具有可逆回复的性质,但是,1700 cm-1处的特征峰在降温再升温过程中几乎没有变化,表明大豆蛋白通过热诱导形成的p-转角构象比较稳定。
蛋白质材料通常在制备后很短时间内(几个小时或者更短的时间)会发生结构的变化,如较容易吸收空气中的水分使其力学性能发生改变,为日后的使用带来很大的不便。因此我们在通过红外光谱考察大豆蛋白膜热诱导其构象转变的基础上,结合热力学分析(TGA和DMTA)从分子水平上来重点讨论水在大豆蛋白膜构象转变中的作用。结合这三种不同的测试方法进行动力学分析,我们发现大豆蛋白膜的构象转变速率与蛋白质热力学次级松弛过程中的其分子链氨基酸残基上缔合的水分子经升温后的脱离过程有密切联系。在加热过程中,随着水分子活动能力的增加,蛋白质主链上氨基酸残基的氢键被破坏,取而代之的是脱离水分子后的氨基酸残基间形成了新的氢键,从而引起蛋白质分子链的构象转变。但是我们的研究表明,简单的水蒸发过程并不能提供足够的活化能使蛋白质分子链发生重排,而是蛋白质变性或其玻璃化转变过程中水与氨酸残基之间相互作用引起的弹性不稳定状态导致了其从无序结构向有序结构转变。
在研究大豆蛋白构象转变机理的同时,制备纯天然大豆蛋白材料是本论文的另一研究目的。虽然大豆蛋白在膜材料、纤维和塑料领域有一定的应用,但是将其作为智能型水凝胶方面的应用却未见报道。由于大豆蛋白的分子链上含有较多的酸性和碱性氨基酸残基,具有相当数量的可离子化基团,因此,我们成功将其制备成了一种具有较好力学性能的电场敏感水凝胶。作为一种蛋白质水凝胶,大豆蛋白水凝胶上所带电荷的种类和数量取决于电解质溶液的pH值及其本身的等电点。当pH值接近大豆蛋白质等电点时,大豆蛋白凝胶上所带的电荷数量非常少,因此在pH=6的电解质溶液中大豆蛋白水凝胶几乎没有电场响应性。在pH<6的缓冲溶液中,大豆蛋白水凝胶具有聚阳离子的性质,在电场的作用下弯向阳极；在pH>6的缓冲溶液中,该水凝胶变为聚阴离子,在电场的作用下弯向阴极。在pH=2-4和pH=10-12范围内,水凝胶的平衡弯曲角可以达到60°以上,甚至在pH=2以及pH=12时,电压为20 V的条件下可以达到90°。另外,在pH=7的中性条件下,大豆蛋白水凝胶弯向阴极,电压为20 V时平衡弯曲角度可以达到21°。这些结果表明了我们制备的大豆蛋白水凝胶是一种性能良好的天然高分子电场敏感水凝胶,在很宽的pH值范围均具有较好的电场响应性,优于我们课题组先前报道的壳聚糖/羧甲基纤维素水凝胶和壳聚糖/羧甲基壳聚糖水凝胶。除溶液的pH值外,电压的大小、溶液的离子强度等都会影响大豆蛋白水凝胶的电场响应性,并且大豆蛋白水凝胶的弯曲行为具有很好的重复性,这些特点表明该水凝胶在微型传感器、微型驱动器以及人工肌肉方面具有潜在的应用价值。此外,在环形电场刺激下,大豆蛋白水凝胶环也有很好的刺激响应性,拓展了其应用范围,为日后大豆蛋白电场敏感水凝胶的实际应用奠定了基础。
综上所述,我们首先获得了分子链未降解的高浓度大豆蛋白溶液,然后采用流变技术测定了其溶液性质,用红外光谱研究了其构象转变,同时结合热力学分析,提出了大豆蛋白在热诱导下的构象转变机理。最后我们成功制备了一种具有相当应用潜力的大豆蛋白电场敏感水凝胶,并详细研究了影响其电场响应性的因素。由此,本论文分别从基础研究和实际应用两方面对大豆蛋白这一种天然高分子材料进行了较为系统的研究,期望能够加深对大豆蛋白这种来源丰富,可资源再生的天然高分子材料的了解,拓展其应用领域。
Soybean has a long history in the food industry owing to its high nutritional value and processability. However, soybean also contains a large fraction of proteins (up to 40%) that has attracted research interests for the development of environment-friendly protein materials with potential excellent physical properties. Soy protein isolate (SPI), more than 90% protein content, contains two major components:glycinin (11S, approximately 52% of the total protein content) and (3-conglycinin (7S, approximately 35% of the total protein content). These two components are responsible for the nutritional, physicochemical and physiological properties of soy proteins. In order to take full advantage of the green feature of soy protein, a fundamental understanding of the relationship between structure and properties of soy protein will be very valuable for the preparation and application of natural protein materials in the future, as well as the more direct application to soy-based foodstuffs and environmentally friendly structural polymers.
Soy protein has complex composition and structure and there are relatively strong interactions in and between the subunits, which prevents soy protein from dissolving in water. Therefore, the preparation of uniform and steady aqueous solution of soy protein is important for further investigation. Herein, two biochemical agents, guandine hydrocholoride (GuIICl) and dithiothreitol (DTT), were used to destroy the hydrogen bonds and disulfide bonds in soy protein, which were removed by dialysis against water to obtain soy protein solution with initial concentration of 3.0 wt% and without obvious degradation. More concentrated soy protein solutions were obtained by reverse dialysis against PEG solution. It is essential to know the properties of soy protein solution for fully understanding and improving the structure and properties of soy protein. So rheological measurements were applied to study the properties of soy protein solution with different concentrations. When the concentration was equal to or lesser than 7.2 wt%, the modulus were independent on the concentrations of soy protein solution and the storage modulus were higher than the loss modulus in low frequency, observations revealed the existence of some microgel structure. However, there was a significant change when the concentration was equal to or higher than 9.0 wt%, the dynamic modulus and the frequency conformed to the following relations:G′(ω)～G″(ω)～ωn, fitting in with Winter's self-similar relaxation line model, that is, when the concentration is equar to the critical concentration 11.3 wt% it can form an metastable critical gel; otherwise, when the concentration is lower than 11.3 wt% it changed to solution while weak gel could form when the concentration is higher than 11.3 wt%.
The functions of soy protein are closely related to its conformation and aggregation structure, so the thermally-induced conformational transitions of soy protein films were studied detailedly and corresponding mechanism of conformational changes was proposed. In the heating process, the heat energy made the soy protein molecular chain segment move with partial adjustment or rearrangement, some volatile random coil structure destructed and formed a relatively stable P-turn conformation. We also suggested that the peak at 1500 cm-1 was assigned to the characteristic of p-turn with the homologous at the peak of 1700 cm-1 according to FTIR and 2D-IR. The rate of change in amide I was faster than at the peak of 1550 cm-1 because of the combination mode of amide II and Tyrosine. The mechanism of conformational transitions of soybean protein films under isothermal conditions was the same as in the heating process. Moreover, the observations in heated-cooled-heated experiment revealed that about 30%～40 %conformation could be reversible, however, the peak at 1700 cm-1 had little change which showed that the heating-inducedβ-turn conformation was very stable.
Generally speaking, properties such as water pick-up and mechanical properties of protein materials are often seen to change significantly over a period of minutes or hours after preparation, even under moderate laboratory conditions around ambient temperature. So we tried to study the effect of water on the thermally-induced conformational transitions of soy protein films. By comparing the kinetics of protein-water interactions as a function of temperature using time resolved FTIR, TGA, and DTMA measurements on soybean protein films, we found that simply evaporating water from the film (TGA) is insufficient to explain the rate of conformational changes (FTIR and DMTA). The onset of mobility in the water molecules allows the amide groups to reconfigure and form stronger amide-amide hydrogen bonds. Thus, simple loss of water (evaporation) is insufficient by itself to allow the protein chains to reconfigure, which requires an activation step for the water to become mobile. We suggest that an elastic instability condition of denaturation or glass transition events in water-amide interactions is the governing mechanism for conformational changes that allows the evolution of disordered structures into more ordered secondary structures, thereby controlling the changes in physical properties such as stiffness and water sensitivity.
Owing to its sustainability, abundance, low cost and functionality, soy protein has attracted great research interests for the development of environment-friendly protein materials with potentially good properties, such as regeneration, biocompatibility and biodegradability, etc. To date, numerous soy protein-based materials have been studied which can be divided into plastics, gels, films, and additives or coatings. However, there have not been any studies on electroactive protein hydrogels made of pristine soy protein. A natural electroactive protein hydrogel was prepared from soy protein isolate (SPI) solution by crosslinking with epichlorohydrin. Under electrical stimulus, such SPI hydrogel quickly bends towards one electrode, showing a good electroactivity. Because of its amphoteric nature, the SPI hydrogel bends either toward the anode (pH< 6) or cathode (pH> 6), depending on the pH of the electrolyte solution. Other factors, such as electric field strength and ionic strength also influence the electromechanical behavior of the SPI hydrogels. Moreover, this SPI hydrogel exhibits a good electroactive behavior under strong acidic (pH=2-4) or basic (pH=10-12) solutions, which is a significant improvement over two other kinds of natural electroactive hydrogels, i.e., chitosan/carboxymethylcellulose and chitosan/carboxymethylchitosan hydrogel, which we reported previously. The wide pH range and good electroactivity of this natural protein hydrogel suggests its great potential for microsensor and actuator applications, especially in the biomedical field, and also to increase the scope of natural polymer-based electroactive hydrogels.
In conclusion, we first obtained high concentrated soy protein solution without obvious degradation and also studied the properties of this solution by rheological measurements. Then, we studied the thermally-induced conformational transitions of soy protein films detailedly by FTIR and thermodynamic analysis and suggested the mechanism of conformational changes. At last, we successfully prepared a natural electroactive protein hydrogel from soy protein solution by crosslinking with epichlorohydrin. Thus, in this thesis, we systematically studied the soy protein in both the basic research and its practical application, so as to learn more about the soy protein from the perspective of bipolymer and finally expand its applications.
引文
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