【摘要】：凝膠性是大豆蛋白最突出的功能性質(zhì)之一,為食品體系貢獻彈性、硬度、持水性、風味成分保留等功能。目前,凝膠型大豆蛋白在肉制品、千葉豆腐、魚糜制品等產(chǎn)品中應用廣泛。認識凝膠結(jié)構(gòu)、了解凝膠結(jié)構(gòu)和性質(zhì)的關系,對凝膠型大豆蛋白產(chǎn)品的開發(fā)和應用均有理論和實際指導意義。本論文從確定大豆蛋白凝膠中網(wǎng)絡蛋白和非網(wǎng)絡蛋白的組成入手,通過研究非網(wǎng)絡成分的擴散行為以及凝膠的質(zhì)構(gòu)、流變和微觀結(jié)構(gòu)特性,對凝膠網(wǎng)絡結(jié)構(gòu)進行了表征;同時通過測定蛋白質(zhì)的組成、網(wǎng)絡蛋白的濃度和網(wǎng)絡蛋白之間相互作用力的變化,揭示了凝膠網(wǎng)絡結(jié)構(gòu)變化的原因。首先,采用擴散法對凝膠中非網(wǎng)絡蛋白和網(wǎng)絡蛋白進行了分離,通過不同電泳技術對兩類蛋白質(zhì)的組成及存在形式進行了分析。以18%(w/v)蛋白質(zhì)溶液在0.1 nol/L鹽離子濃度和95℃條件加熱30 min形成的大豆蛋白凝膠中的非網(wǎng)絡蛋白為代表,其主要組成是11S的A、B肽鏈和胰凝乳蛋白酶抑制劑(BBI),此外含有少量的7S-α’、α亞基。其中B肽鏈以AB和A5B3的形式存在;A肽鏈除了這兩種形式外,還包含單體、二聚體、三聚體和聚合體等形式;BBI以單體形式存在。針對網(wǎng)絡蛋白組成的研究,討論中結(jié)合分析了三種蛋白凝膠中的網(wǎng)絡蛋白。其中,7S-α、α’亞基通過形成聚集體和多聚體兩種形式參與到凝膠網(wǎng)絡結(jié)構(gòu)中;7S-β亞基是以聚集體的形式參與到凝膠網(wǎng)絡結(jié)構(gòu)中。11S-A3、A肽鏈主要以二硫鍵連接的聚合體的形式參與到凝膠網(wǎng)絡結(jié)構(gòu)中,而11SB肽鏈可以以單體、二聚體、聚合體、聚集體等形式參與到凝膠網(wǎng)絡中。在此基礎上,繼續(xù)研究了非網(wǎng)絡蛋白的擴散行為和凝膠結(jié)構(gòu)變化的關系;并通過分析非網(wǎng)絡蛋白和網(wǎng)絡蛋白的組成及含量的變化,揭示了凝膠網(wǎng)絡結(jié)構(gòu)變化的原因。排阻色譜分析表明非網(wǎng)絡蛋白由三部分組成,相對分子質(zhì)量分別為253.9、44.8和9.7 kDa;三種成分在起始階段的擴散符合Fick第二定律。制備凝膠時的蛋白質(zhì)濃度增加或加熱時間延長可引起非網(wǎng)絡蛋白擴散系數(shù)的降低。擴散系數(shù)與相對分子質(zhì)量之間符合冪次函數(shù)關系,其中特征指數(shù)因子α值隨著蛋白質(zhì)濃度增加、加熱時間延長而變大,說明凝膠網(wǎng)絡結(jié)構(gòu)趨于致密。電泳和蛋白質(zhì)濃度分析結(jié)果表明,11S蛋白變性程度和網(wǎng)絡蛋白含量的增加是導致凝膠網(wǎng)絡結(jié)構(gòu)致密的原因。進一步通過研究外源性分子探針的擴散考察了7S/11S比率和鹽濃度對凝膠網(wǎng)絡結(jié)構(gòu)的影響;并采用掃描電子顯微鏡對擴散實驗結(jié)果進行了驗證。在同一條件下制備的蛋白質(zhì)凝膠中,探針的相對分子質(zhì)量越大擴散系數(shù)越小;在不同的蛋白質(zhì)凝膠中,探針相對分子質(zhì)量越大,其擴散對凝膠網(wǎng)絡結(jié)構(gòu)的變化越敏感。凝膠中探針的擴散系數(shù)隨著鹽離子濃度或總蛋白中11S比率的增加而增大;掃描電子顯微鏡數(shù)據(jù)結(jié)果顯示,隨著鹽離子濃度或11S比率增加,凝膠網(wǎng)絡結(jié)構(gòu)孔隙變大、蛋白質(zhì)聚集體分布不均勻,導致探針在網(wǎng)絡結(jié)構(gòu)中容易擴散。通過測定凝膠在SDS溶液或SDS和DTT混合溶液中溶解速率,對凝膠網(wǎng)絡蛋白中分子間作用力的類型和大小進行了表征,并與凝膠破裂力的測定結(jié)果進行了比較。結(jié)果表明,疏水、氫鍵相互作用和二硫鍵均參與了大豆蛋白凝膠網(wǎng)絡結(jié)構(gòu)的形成;作用力強弱的變化與凝膠破裂力大小的變化呈正相關。隨著總蛋白中11S比率增加或加熱溫度升高,凝膠中疏水、氫鍵相互作用和二硫鍵均加強,凝膠破裂力的值逐漸增大;隨著加熱時間的延長,網(wǎng)絡蛋白分子間相互作用和凝膠破裂力均呈現(xiàn)先增大后減小的變化趨勢。此外,對比發(fā)現(xiàn)加熱溫度對三個作用力的影響最大,加熱溫度變化對凝膠破裂力影響更為顯著。最后研究了大豆蛋白凝膠的彈性模量與非網(wǎng)絡蛋白、網(wǎng)絡蛋白含量以及蛋白質(zhì)聚集體大小的關系。通過擴散法去除凝膠中的非網(wǎng)絡蛋白,對去除前后凝膠彈性模量進行了測定,發(fā)現(xiàn)非網(wǎng)絡蛋白對凝膠彈性模量沒有貢獻。隨著加熱溫度升高,11S蛋白變性程度增加,網(wǎng)絡蛋白占總蛋白的比率增加,進而導致凝膠彈性模量呈指數(shù)性增加。鹽離子濃度和7S/11S比率對凝膠彈性模量的影響不完全取決于網(wǎng)絡蛋白占總蛋白比率,此時凝膠彈性模量與蛋白質(zhì)聚集體的平均粒徑呈正相關。
[Abstract]:Gelatin is one of the most outstanding functional properties of the soybean protein, which is the function of the food system's contribution to elasticity, hardness, water-holding property and flavor component retention. At present, the gel-type soybean protein is widely used in the products such as meat products, bean curd, minced fish products and the like. To understand the gel structure, to understand the relationship between the structure and properties of the gel, the development and application of the gel-type soybean protein product are both theoretical and practical. Based on the determination of the composition of the network protein and the non-network protein in the soybean protein gel, the gel network structure was characterized by studying the diffusion behavior of the non-network component and the properties of the texture, the rheological and the microstructure of the gel, and the composition of the protein was also determined. The change of the interaction force between the concentration of the network protein and the network protein reveals the cause of the change of the gel network structure. First, the non-network protein and the network protein in the gel were separated by the diffusion method, and the composition and the existing form of the two kinds of proteins were analyzed by different electrophoretic techniques. The non-network protein in the soy protein gel, which was formed by heating for 30 min at a concentration of 0.1 mol/ L and at 95.degree. C. with an 18% (w/ v) protein solution, was represented by a peptide chain of 11S and a chymotrypsin inhibitor (BBI), in addition to a small amount of 7S-1. ', sub-subunit. in which the B-chain is present in the form of AB and A5B3; in addition to these two forms, the peptide chain also contains the form of monomers, dimers, trimers, and polymers; and the BBI is present in the form of a monomer. In order to study the network protein composition, the network protein in three kinds of protein gel was analyzed in the paper. Of which, 7S-1, 1' the subunits are involved in the gel network structure by forming aggregates and multimers; the 7s-subunits are in the form of aggregates that are involved in the gel network structure, The 11SB peptide chain may be incorporated into the gel network in the form of monomers, dimers, polymers, aggregates, and the like. On this basis, the relationship between the non-network protein's diffusion behavior and the change of the gel structure was studied, and the reason of the change of the gel network structure was revealed by analyzing the composition and the content of the non-network protein and the network protein. The analysis of exclusion chromatography showed that the non-network protein was composed of three parts, and the relative molecular weight was 253.9, 42.8 and 9.7kDa, respectively. The diffusion of the three components in the initial stage was in accordance with the Fick's second law. The increase in protein concentration or prolonged heating time during the preparation of the gel may result in a decrease in the non-network protein diffusion coefficient. The relationship between the diffusion coefficient and the relative molecular mass is a power-order function, wherein the value of the characteristic index factor is increased with the increase of the concentration of the protein, the heating time is prolonged, and the gel network structure tends to be compact. The results of the analysis of electrophoresis and protein concentration show that the degree of denaturation of 11S protein and the increase of the content of the network protein are the cause of the dense structure of the gel network. The effect of the ratio of 7S/ 11S and the salt concentration on the structure of the gel was further investigated by the study of the diffusion of the exogenous molecular probe, and the results of the diffusion experiment were verified by the scanning electron microscope. In the protein gel prepared under the same condition, the greater the relative molecular mass of the probe and the smaller the diffusion coefficient of the relative molecular mass of the probe, the greater the relative molecular mass of the probe in different protein gels, the more sensitive the diffusion of the probe to the gel network structure. the diffusion coefficient of the probe in the gel is increased with the increase of the concentration of the salt ions or the 11S ratio in the total protein; the scanning electron microscope data show that as the concentration of the salt or the 11S ratio increases, the pore of the gel network structure becomes large, the distribution of the protein aggregates is not uniform, resulting in an easy diffusion of the probe in the network structure. The type and size of the intermolecular force in the gel network protein were characterized by measuring the dissolution rate of the gel in the SDS solution or SDS and the DTT mixed solution, and compared with the determination result of the gel breaking force. The results showed that both the hydrophobic, hydrogen bond interaction and the disulfide bond were involved in the formation of the network structure of the soybean protein gel; the change of the strength of the acting force was positively related to the change of the gel breaking force. As the 11S ratio in the total protein is increased or the heating temperature is increased, the hydrophobic, hydrogen bond interaction and the disulfide bond in the gel are enhanced, the value of the gel breaking force is gradually increased, and as the heating time is prolonged, The interaction between the network protein molecules and the gel breaking force exhibit a tendency to decrease after the first increase. In addition, the effect of the heating temperature on the three forces was found to be the largest, and the change of the heating temperature was more significant to the gel breaking force. The relationship between the elastic modulus of the soybean protein gel and the non-network protein, the content of the network protein and the size of the protein aggregates was studied. The non-network protein in the gel was removed by the diffusion method, and the elastic modulus of the gel before and after removal was measured, and the non-network protein was found to have no contribution to the elastic modulus of the gel. As the temperature of the heating increases, the degree of denaturation of the 11S protein increases, and the ratio of the network protein to the total protein is increased, resulting in an exponential increase in the elastic modulus of the gel. The effect of the salt ion concentration and the ratio of 7S/ 11S on the elastic modulus of the gel is not entirely dependent on the total protein ratio of the network protein, at which point the elastic modulus of the gel is positively related to the average particle size of the protein aggregate.
【學位授予單位】：江南大學
【學位級別】：博士
【學位授予年份】：2017
【分類號】：TS201.21

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