核桃蛋白质的结构表征及其制品的改性研究
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摘要
我国核桃种植和产量居全世界第一位。核桃除部分出口和国内鲜食销售外，主要加工成核桃油、核桃粉、核桃乳等产品。在核桃油生产的过程中产生了大量的核桃脱脂粕，由于各地核桃提油方法的不同，造成脱脂粕的成分复杂，蛋白质功能性差，致使核桃蛋白质很难广泛的应用到食品加工中，从而造成了蛋白质资源的浪费。为了能有效利用这一植物蛋白质资源，扩大核桃蛋白质产品在食品加工及其它领域的应用范围，本课题对核桃蛋白质的结构表征及其制品的改性进行了研究，深入考察了核桃蛋白质及其分离组分的组成与结构，核桃蛋白质分离提取及制备与等电点，核桃分离蛋白和浓缩蛋白的结构与功能性以及有限酶水解核桃分离蛋白的机理。
对核桃蛋白质及其分离组分的重要物理化学参数进行了表征，深入研究了核桃蛋白质的组成与结构。结果显示，核桃蛋白质进行组分分离得到清蛋白、球蛋白、醇溶蛋白、谷蛋白，其含量分别是7.54%，15.67%，4.73%，72.06%。谷蛋白是构成核桃蛋白组成的主要部分。核桃脱脂粉和核桃蛋白分离组分的氨基酸组成中，以谷氨酸、精氨酸、天冬氨酸含量较高，且主要以酸性氨基酸和疏水性氨基酸为主，赖氨酸是核桃脱脂粉、清蛋白、球蛋白、谷蛋白的第一限制氨基酸，而亮氨酸为醇溶蛋白的第一限制性氨基酸。核桃脱脂粉的分子量分布比较宽，其分子量分布范围是3.54kDa~81.76kDa之间。其中，球蛋白在11.25kDa~78.60kDa之间，谷蛋白在14.25kDa左右，清蛋白在3.63kDa~67.14kDa之间，醇溶蛋白在13.17kDa左右。核桃蛋白质的亚基组成比较复杂，非还原电泳图显示有11个条带，分子量范围在14kDa~120kDa之间，还原条件下肽链分子量范围在14kDa~60kDa之间，其中，相对分子量为30kDa~43kDa和20kDa~28kDa的为酸性肽链，相对分子量为14.4kDa~20.1kDa的为碱性肽链。球蛋白显示有9个条带，分子量范围在20kDa~120kDa之间；清蛋白显示有8个条带，分子量范围在14kDa~60kDa之间；谷蛋白显示有5个条带，分子量范围在14kDa~60kDa之间。核桃蛋白分离组分的电泳条带分子量范围与核桃蛋白质基本吻合。核桃蛋白的组成蛋白等电点主要集中在pI4.8~6.8之间，即以酸性蛋白为主，少数的蛋白是碱性蛋白，pI8.4~9.0。
通过对核桃蛋白质分离提取及等电点的研究，确定了核桃分离蛋白和浓缩蛋白的制备工艺。结果显示，对比烘烤法、热烫法、碱液浸泡法等核桃仁去皮方法的去皮效果，以碱液法去皮效果最好，即先将核桃仁在水中浸泡0.5h，然后在2%NaOH溶液中浸泡4min。在各种因素中，提取pH对核桃蛋白提取率影响最大。固定提取pH11，采用响应面法优化得到核桃蛋白提取最佳条件为：料液比1:26（w/v）、提取温度53℃、提取时间1.5h，提取率达82.68%。确定了核桃碱溶蛋白的酸沉点为pH4.5。按照本实验的工艺制备的核桃分离蛋白和浓缩蛋白，纯度分别为90.50%、75.56%，均比其他工艺制备的核桃蛋白纯度高。
对核桃分离蛋白和浓缩蛋白的结构进行表征，同时系统研究了核桃分离蛋白和浓缩蛋白的化学组成、表面疏水性和功能特性。结果显示，核桃分离蛋白和浓缩蛋白的二级结构含量比较相似，在制备过程中使核桃蛋白质的二级结构发生了变化，α-螺旋结构受到一定程度的破坏，β-转角和无规则卷曲结构显著增加，β-折叠少量增加。核桃分离蛋白的分子量分布相对单一，分子量集中在89.6kDa左右。核桃浓缩蛋白的分子量集中在11kDa~79kDa之间，较为复杂。核桃分离蛋白和浓缩蛋白的制备工艺对核桃蛋白质的氨基酸破坏不显著，尤其对于胱氨酸和蛋氨酸等含硫氨基酸影响不大。核桃分离蛋白显示出比较稀松的大片层结构，而核桃浓缩蛋白显示出较小且更为紧实的片层结构。这种大的片层结构有助于提高核桃蛋白的溶解度。pH和NaCl浓度对核桃分离蛋白和浓缩蛋白的溶解性、乳化特性、起泡特性都有显著的影响。在碱性pH条件下比在酸性pH条件下更能提高蛋白质的溶解性、乳化特性和起泡特性。低浓度的NaCl（0.1~1.0mol/L）可以提高分离蛋白和浓缩蛋白的溶解度、乳化特性和起泡特性。分离蛋白的溶解度、乳化稳定性、起泡特性显著高于浓缩蛋白。中性条件下，分离蛋白的吸油性显著高于浓缩蛋白，二者的吸油性均大于大豆分离蛋白，而吸水性低于浓缩蛋白。
采用Alcalase碱性蛋白酶对核桃分离蛋白进行有限酶水解，探索了有限酶水解核桃分离蛋白的机理，并获得了较好功能性的酶水解方法。结果显示，采用响应面法优化得到的Alcalase蛋白酶酶解核桃分离蛋白的最佳水解条件，即pH8.7，加酶量0.05%（mL/g），底物浓度5.0%，温度55℃。发现适度酶解可以提高酶解物的表面疏水性，改变了二级结构，使分子量减小并分散，增加疏水性氨基酸，减少亲水性氨基酸，使酸性肽链先水解，碱性肽链不水解，使大的片层结构变为夹杂着小颗粒的小片层结构，反映在功能性上则表现为提高核桃分离蛋白的氮溶解度指数，乳化性、乳化稳定性及起泡性、泡沫稳定性及吸水性和吸油性。从提高氮溶解度指数和乳化特性的角度考虑，采用Alcalase蛋白酶水解核桃分离蛋白，选取6%水解度能显著提高核桃分离蛋白功能性。
China’s walnut cultrivation area and output rank first in the world. Except for exports asfresh food and domestic sales, walnuts are mainly processed into products, like walnut oil,walnut powder and walnut milk. Walnut oil production produces a lot of defatted walnut flour.Because of different walnut oil extraction methods, the component of defatted walnut flourwas complex and function was poor, leading walnut protein is hard to wide application infood processing. In order to make effective use of plant proteins in this resource and toexpand the fields of walnut protein products in food processing and other applications, theresearch on structure characterization and products’modification of walnut protein wasconducted in this article. Structure and properties of walnut protein, walnut protein extractioncondition and isoelectric point, development of walnut protein isolate and concentrate and onlimited enzymatic hydrolysis of walnut protein isolate to improvement functionality weredeeply investigated.
Important physical chemistry parameters characterization, structure and properties ofwalnut protein and protein fractions were deeply investigated. Results showed that walnutprotein fractions are albumin, prolamin, glutelin and globulin with content of7.54%,4.73%,72.06%,15.67%, respectively. Glutelin was the main protein composition of walnut. Thecontent of glutamic acid, arginine, aspartic acid was the highest in the amino acidescomposition of walnut protein and protein fractions and dominated by acidic amino acids andhydrophobic amino acid. Lysine was the first limiting amino acids of defatted walnut flour,albumin, glutelin and globulin and Leucine was the first limiting amino acids of prolamin.Molecular weight distribution of defatted walnut flour was broad with the range of3.54kDa~81.76kDa and molecular weight distribution of globulin, glutelin, albumin andprolamin was between11.25kDa~78.60kDa,14.25kDa,3.63kDa~67.14kDa,3.63kDa~67.14kDa and13.17KD, respectively. Subunits composition of walnut protein wascomplex with molecular weight ranging between14kDa~120kDa, and was made up of11bands on the non-reducing condition. The peptides with molecular weight between31kDa~43kDa and20kDa~28kDa was acid peptides and molecular weight between14.4kDa~20.1kDa was basic peptide. Globulin was made up of9bands, with molecularweight ranging between20kDa~120kDa. Albumin was made up of8bands, with molecularweight ranging between14kDa~60kDa. Glutelin was made up of5bands, with molecularweight ranging between14kDa~60kDa. The subunit composition of walnut protein fractionsand walnut protein were basically. By two-dimensional gel electrophoresis study, walnutprotein isoelectric point is mainly concentrated at pI4.8~6.8with few isoelectric pointconcentrated at pI8.4~9.0. Walnut protein was dominated by acidic protein.
The preparation technology of walnut protein isolate and concentrate was determined bystuding the extraction condition and isoelectric point of walnut protein. Peeling methods forwalnut kernel was systematically studied among the methods of roasted, blanching and alkalisolution soaking. Result showed that peeling method of alkali solution soaking was best, with2%NaOH for4min. Among the variety of factors, the extraction rate was influencedeffectively on extraction pH. Optimum extraction conditions results by Response SurfaceMethod for walnut protein was: solid-liquid ratio was1:26(w/v); extraction temperature was53℃; extraction time was1.5h; extraction rate was82.68%. It was determined that the isoelectric point of alkali-soluble protein of walnut protein was pH4.5. The purity of walnutprotein isolates and concentrates prepared by above preparation technology was90.50%,75.56%, respectively, which are higher than walnut protein products produced by othertechniques.
The protein structure and chemical composition, surface hydrophobicity, functionalproperties of walnut protein isolate and concentrate was systematicly studied with view toexploring protein structure and functional relationships. The secondary structure content ofwalnut protein concentrate and isolate was similar. It was showed that the secondary structureof walnut protein concentrate and isolate were changed during preparateion, with destructionof α-helix structure, significant increased of β-turns, random coil structure and a small amountincrease of β-sheet. Results showed that the molecular weight distribution of walnut proteinisolate was relatively single with molecular weight at89.6kDa. However, the molecularweight distribution of walnut protein concentrate was more complicated about11kDa~79kDa.The amino acids were not damaged through preparation of walnut protein concentrate andisolate, especially for cysteine and methionine. Walnut protein isolate showed relatively weaklarge-layer structure. However, walnut protein concentrates showed layers of smaller andmore compact structure. It was suggeseted that large-layer structure helps to increase thesolubility of walnut protein. Solubility and emulsifying property, foaming property of walnutprotein isolate and concentrate was significantly influenced by pH and NaCl concentrations.Low concentrations of NaCl (0.1~1.0mol/L) can improve the solubility, emulsifyingproperties and foaming properties of walnut protein isolate and concentrate. Solubility,emulsifying properties and foaming properties of walnut protein isolate was significantlyhigher than that of walnut protein concentrate, which was due to the difference onmicro-structure, molecular weight distribution and components. Under neutral conditions, fatabsorption capacity of walnut protein isolate was significantly higher than protein concentrate,which all were higher than that of soy protein isolate. Water absorption capacity of walnutprotein isolate was less than protein concentrate.
Walnut protein isolate was limitedly hydrolyzed by Alcalase alkaline protease. Thecomposition, structure and functional properties of hydrolysate were systematically studied.Optimize conditions of enzymatic hydrolysis by response surface methodology was: pH8.7,enzyme0.05%(mL/g),5%substrate concentration, temperature is55℃. The results showedthat moderate hydrolysis can increase surface hydrophobicity, change secondary structure,makes molecular weight decrease and disperse, increase hydrophobic amino acids, reducehydrophilic amino acids, makes acid peptide hydrolysis first and alkaline peptide does nothydrolysis, make large layer structure becomes small layer structure with small particles. Thehydrolysates changes above can improve the nitrogen solubility index, emulsifying stability,foaming properties, fat absorption capacity and water absorption capacity. Walnut proteinisolate through limited hydrolyzed by Alcalase showed better functional properties with DHof6%form the perspective of improving nitrogen solubility index and emulsifying properties.
对核桃蛋白质及其分离组分的重要物理化学参数进行了表征，深入研究了核桃蛋白质的组成与结构。结果显示，核桃蛋白质进行组分分离得到清蛋白、球蛋白、醇溶蛋白、谷蛋白，其含量分别是7.54%，15.67%，4.73%，72.06%。谷蛋白是构成核桃蛋白组成的主要部分。核桃脱脂粉和核桃蛋白分离组分的氨基酸组成中，以谷氨酸、精氨酸、天冬氨酸含量较高，且主要以酸性氨基酸和疏水性氨基酸为主，赖氨酸是核桃脱脂粉、清蛋白、球蛋白、谷蛋白的第一限制氨基酸，而亮氨酸为醇溶蛋白的第一限制性氨基酸。核桃脱脂粉的分子量分布比较宽，其分子量分布范围是3.54kDa~81.76kDa之间。其中，球蛋白在11.25kDa~78.60kDa之间，谷蛋白在14.25kDa左右，清蛋白在3.63kDa~67.14kDa之间，醇溶蛋白在13.17kDa左右。核桃蛋白质的亚基组成比较复杂，非还原电泳图显示有11个条带，分子量范围在14kDa~120kDa之间，还原条件下肽链分子量范围在14kDa~60kDa之间，其中，相对分子量为30kDa~43kDa和20kDa~28kDa的为酸性肽链，相对分子量为14.4kDa~20.1kDa的为碱性肽链。球蛋白显示有9个条带，分子量范围在20kDa~120kDa之间；清蛋白显示有8个条带，分子量范围在14kDa~60kDa之间；谷蛋白显示有5个条带，分子量范围在14kDa~60kDa之间。核桃蛋白分离组分的电泳条带分子量范围与核桃蛋白质基本吻合。核桃蛋白的组成蛋白等电点主要集中在pI4.8~6.8之间，即以酸性蛋白为主，少数的蛋白是碱性蛋白，pI8.4~9.0。
通过对核桃蛋白质分离提取及等电点的研究，确定了核桃分离蛋白和浓缩蛋白的制备工艺。结果显示，对比烘烤法、热烫法、碱液浸泡法等核桃仁去皮方法的去皮效果，以碱液法去皮效果最好，即先将核桃仁在水中浸泡0.5h，然后在2%NaOH溶液中浸泡4min。在各种因素中，提取pH对核桃蛋白提取率影响最大。固定提取pH11，采用响应面法优化得到核桃蛋白提取最佳条件为：料液比1:26（w/v）、提取温度53℃、提取时间1.5h，提取率达82.68%。确定了核桃碱溶蛋白的酸沉点为pH4.5。按照本实验的工艺制备的核桃分离蛋白和浓缩蛋白，纯度分别为90.50%、75.56%，均比其他工艺制备的核桃蛋白纯度高。
对核桃分离蛋白和浓缩蛋白的结构进行表征，同时系统研究了核桃分离蛋白和浓缩蛋白的化学组成、表面疏水性和功能特性。结果显示，核桃分离蛋白和浓缩蛋白的二级结构含量比较相似，在制备过程中使核桃蛋白质的二级结构发生了变化，α-螺旋结构受到一定程度的破坏，β-转角和无规则卷曲结构显著增加，β-折叠少量增加。核桃分离蛋白的分子量分布相对单一，分子量集中在89.6kDa左右。核桃浓缩蛋白的分子量集中在11kDa~79kDa之间，较为复杂。核桃分离蛋白和浓缩蛋白的制备工艺对核桃蛋白质的氨基酸破坏不显著，尤其对于胱氨酸和蛋氨酸等含硫氨基酸影响不大。核桃分离蛋白显示出比较稀松的大片层结构，而核桃浓缩蛋白显示出较小且更为紧实的片层结构。这种大的片层结构有助于提高核桃蛋白的溶解度。pH和NaCl浓度对核桃分离蛋白和浓缩蛋白的溶解性、乳化特性、起泡特性都有显著的影响。在碱性pH条件下比在酸性pH条件下更能提高蛋白质的溶解性、乳化特性和起泡特性。低浓度的NaCl（0.1~1.0mol/L）可以提高分离蛋白和浓缩蛋白的溶解度、乳化特性和起泡特性。分离蛋白的溶解度、乳化稳定性、起泡特性显著高于浓缩蛋白。中性条件下，分离蛋白的吸油性显著高于浓缩蛋白，二者的吸油性均大于大豆分离蛋白，而吸水性低于浓缩蛋白。
采用Alcalase碱性蛋白酶对核桃分离蛋白进行有限酶水解，探索了有限酶水解核桃分离蛋白的机理，并获得了较好功能性的酶水解方法。结果显示，采用响应面法优化得到的Alcalase蛋白酶酶解核桃分离蛋白的最佳水解条件，即pH8.7，加酶量0.05%（mL/g），底物浓度5.0%，温度55℃。发现适度酶解可以提高酶解物的表面疏水性，改变了二级结构，使分子量减小并分散，增加疏水性氨基酸，减少亲水性氨基酸，使酸性肽链先水解，碱性肽链不水解，使大的片层结构变为夹杂着小颗粒的小片层结构，反映在功能性上则表现为提高核桃分离蛋白的氮溶解度指数，乳化性、乳化稳定性及起泡性、泡沫稳定性及吸水性和吸油性。从提高氮溶解度指数和乳化特性的角度考虑，采用Alcalase蛋白酶水解核桃分离蛋白，选取6%水解度能显著提高核桃分离蛋白功能性。
China’s walnut cultrivation area and output rank first in the world. Except for exports asfresh food and domestic sales, walnuts are mainly processed into products, like walnut oil,walnut powder and walnut milk. Walnut oil production produces a lot of defatted walnut flour.Because of different walnut oil extraction methods, the component of defatted walnut flourwas complex and function was poor, leading walnut protein is hard to wide application infood processing. In order to make effective use of plant proteins in this resource and toexpand the fields of walnut protein products in food processing and other applications, theresearch on structure characterization and products’modification of walnut protein wasconducted in this article. Structure and properties of walnut protein, walnut protein extractioncondition and isoelectric point, development of walnut protein isolate and concentrate and onlimited enzymatic hydrolysis of walnut protein isolate to improvement functionality weredeeply investigated.
Important physical chemistry parameters characterization, structure and properties ofwalnut protein and protein fractions were deeply investigated. Results showed that walnutprotein fractions are albumin, prolamin, glutelin and globulin with content of7.54%,4.73%,72.06%,15.67%, respectively. Glutelin was the main protein composition of walnut. Thecontent of glutamic acid, arginine, aspartic acid was the highest in the amino acidescomposition of walnut protein and protein fractions and dominated by acidic amino acids andhydrophobic amino acid. Lysine was the first limiting amino acids of defatted walnut flour,albumin, glutelin and globulin and Leucine was the first limiting amino acids of prolamin.Molecular weight distribution of defatted walnut flour was broad with the range of3.54kDa~81.76kDa and molecular weight distribution of globulin, glutelin, albumin andprolamin was between11.25kDa~78.60kDa,14.25kDa,3.63kDa~67.14kDa,3.63kDa~67.14kDa and13.17KD, respectively. Subunits composition of walnut protein wascomplex with molecular weight ranging between14kDa~120kDa, and was made up of11bands on the non-reducing condition. The peptides with molecular weight between31kDa~43kDa and20kDa~28kDa was acid peptides and molecular weight between14.4kDa~20.1kDa was basic peptide. Globulin was made up of9bands, with molecularweight ranging between20kDa~120kDa. Albumin was made up of8bands, with molecularweight ranging between14kDa~60kDa. Glutelin was made up of5bands, with molecularweight ranging between14kDa~60kDa. The subunit composition of walnut protein fractionsand walnut protein were basically. By two-dimensional gel electrophoresis study, walnutprotein isoelectric point is mainly concentrated at pI4.8~6.8with few isoelectric pointconcentrated at pI8.4~9.0. Walnut protein was dominated by acidic protein.
The preparation technology of walnut protein isolate and concentrate was determined bystuding the extraction condition and isoelectric point of walnut protein. Peeling methods forwalnut kernel was systematically studied among the methods of roasted, blanching and alkalisolution soaking. Result showed that peeling method of alkali solution soaking was best, with2%NaOH for4min. Among the variety of factors, the extraction rate was influencedeffectively on extraction pH. Optimum extraction conditions results by Response SurfaceMethod for walnut protein was: solid-liquid ratio was1:26(w/v); extraction temperature was53℃; extraction time was1.5h; extraction rate was82.68%. It was determined that the isoelectric point of alkali-soluble protein of walnut protein was pH4.5. The purity of walnutprotein isolates and concentrates prepared by above preparation technology was90.50%,75.56%, respectively, which are higher than walnut protein products produced by othertechniques.
The protein structure and chemical composition, surface hydrophobicity, functionalproperties of walnut protein isolate and concentrate was systematicly studied with view toexploring protein structure and functional relationships. The secondary structure content ofwalnut protein concentrate and isolate was similar. It was showed that the secondary structureof walnut protein concentrate and isolate were changed during preparateion, with destructionof α-helix structure, significant increased of β-turns, random coil structure and a small amountincrease of β-sheet. Results showed that the molecular weight distribution of walnut proteinisolate was relatively single with molecular weight at89.6kDa. However, the molecularweight distribution of walnut protein concentrate was more complicated about11kDa~79kDa.The amino acids were not damaged through preparation of walnut protein concentrate andisolate, especially for cysteine and methionine. Walnut protein isolate showed relatively weaklarge-layer structure. However, walnut protein concentrates showed layers of smaller andmore compact structure. It was suggeseted that large-layer structure helps to increase thesolubility of walnut protein. Solubility and emulsifying property, foaming property of walnutprotein isolate and concentrate was significantly influenced by pH and NaCl concentrations.Low concentrations of NaCl (0.1~1.0mol/L) can improve the solubility, emulsifyingproperties and foaming properties of walnut protein isolate and concentrate. Solubility,emulsifying properties and foaming properties of walnut protein isolate was significantlyhigher than that of walnut protein concentrate, which was due to the difference onmicro-structure, molecular weight distribution and components. Under neutral conditions, fatabsorption capacity of walnut protein isolate was significantly higher than protein concentrate,which all were higher than that of soy protein isolate. Water absorption capacity of walnutprotein isolate was less than protein concentrate.
Walnut protein isolate was limitedly hydrolyzed by Alcalase alkaline protease. Thecomposition, structure and functional properties of hydrolysate were systematically studied.Optimize conditions of enzymatic hydrolysis by response surface methodology was: pH8.7,enzyme0.05%(mL/g),5%substrate concentration, temperature is55℃. The results showedthat moderate hydrolysis can increase surface hydrophobicity, change secondary structure,makes molecular weight decrease and disperse, increase hydrophobic amino acids, reducehydrophilic amino acids, makes acid peptide hydrolysis first and alkaline peptide does nothydrolysis, make large layer structure becomes small layer structure with small particles. Thehydrolysates changes above can improve the nitrogen solubility index, emulsifying stability,foaming properties, fat absorption capacity and water absorption capacity. Walnut proteinisolate through limited hydrolyzed by Alcalase showed better functional properties with DHof6%form the perspective of improving nitrogen solubility index and emulsifying properties.
引文
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