大豆7S与11S球蛋白分离方法的研究

文章就提取分离低温脱脂大豆粕中大豆7S和11S球蛋白的方法进行了研究.利用SDS-PAGE凝胶电泳来评定不同pH值对分离大豆7S球蛋白和大豆11S球蛋白的纯度的影响.实验结果表明,浸提大豆蛋白的最佳工艺参数为磷酸盐缓冲液浓度为0.02 mol/L、料液比1∶16、浸泡温度45 ℃、pH值为8.5,可得到最高浸提率为89.55%.分离大豆11S球蛋白的最适pH值为6.2,纯度达75.76%;分离大豆7S球蛋白的最适pH值为4.7,纯度达72.99%.     

大豆11S球蛋白提取分离方法研究

以11S球蛋白粗提物中蛋白质含量和纯度为评价指标,比较了Nagano法、Saio法与Thanh法提取分离大豆11S球蛋白的效果,并对Thanh法提取分离大豆11S球蛋白的工艺参数进行了优化。结果表明,Thanh法提取分离大豆11S球蛋白效果较好,Tris-HC l缓冲液是适宜的提取液,最优提取工艺条件为提取时间2h、料液比1∶20、提取温度25℃。     

分离7S和11S大豆球蛋白简便方法

该文研究一种实验室直接分离7S和11S大豆球蛋白简便方法,并讨论影响分离效果的一些因素。发现在本方法中最适分离的pH值范围为6.2～6.4,Tris-HCl缓冲液浓度在不超过0.06M时有助于7S和11S球蛋白的分离,高蛋白质浓度(不大于4％)有利于7S和11S球蛋白分离,而NaCl浓度对这两种球蛋白分离影响比较复杂。     

大豆7S球蛋白和11S球蛋白的研究

主要阐述了大豆7S球蛋白和11S球蛋白的分离富集方法及其主要特性。     

大豆分离蛋白中7S和11S大豆球蛋白的选择性酶解研究

使用胃蛋白酶在温度37℃,pH1.5～4.0范围内,以及木瓜蛋白酶在pH7.0,温度37～80℃范围内对大豆分离蛋白(SPI)进行水解,采用聚丙烯酰胺凝胶电泳技术对水解情况进行分析。结果表明,在37℃和pH1.5～2.5条件下,大豆分离蛋白中的11S大豆球蛋白被胃蛋白酶选择性地水解;在70℃,pH7.0条件下,7S大豆球蛋白被木瓜蛋白酶选择性地水解。      

大豆7S球蛋白和11S球蛋白的研究

主要阐述了大豆 7S球蛋白和 1 1S球蛋白的分离富集方法及其主要特性。     

大豆7S和11S球蛋白的结构和功能性质

主要介绍大豆７Ｓ和１１Ｓ球蛋白的结构和功能性质，大豆蛋白质各个成分的分子量有所不同，按超速离心分离系数可分为２Ｓ，７Ｓ１１Ｓ和１５Ｓ４个组份。７Ｓ组份占总蛋白质的３０．９％，它是由４种不同大豆蛋白民组成，１１Ｓ组份占总大豆蛋白质的４１％，而且都是单一的１１Ｓ球蛋白，１１Ｓ球蛋白的等电点为ｐＨ４．６４。     

大豆11S球蛋白水解肽的制备及抗氧化研究

以大豆11S球蛋白为原料,通过胰蛋白酶水解制备活性肽,在单因素试验的基础上,采用响应面法确定最佳酶解条件,并检测大豆肽溶液的体外抗氧化性。结果表明,底物浓度2 mg/mL时的最佳水解条件为:酶和底物比4 900 U/g,pH8.1,温度44℃,水解时间2.6 h,此条件下经验证试验得到大豆肽的水解度为89.25%。大豆肽溶液对超氧阴离子自由基(O_2~-·)和羟自由基(·OH)都具有良好的清除效果,随着大豆肽溶液浓度的增加,O_2~-·和·OH的清除率也随之增加。当肽液浓度为12 mg/mL时,对O_2~-·的清除率最高达到46.86%;当肽液浓度为0.5 mg/mL时对·OH的清除率最高,达到33.73%。     

7S 伴大豆球蛋白及其糖基化产物对大豆11S 球蛋白热聚集的影响

研究7S 伴大豆球蛋白(β - 伴大豆球蛋白)及其糖基化产物对大豆11S 球蛋白热聚集的影响。从浊度、ξ -电位、粒度、SDS-PAGE 测定得出在30mmol/L Tris-HCl 缓冲溶液中(含β - 巯基乙醇),7S 球蛋白及其糖基化产物能够抑制11S 球蛋白的热聚集,并且糖基化产物的抑制效果比未糖基化的7S 球蛋白明显;7S 球蛋白及其糖基化产物抑制11S 球蛋白热聚集的机理不同,7S 球蛋白糖基化产物对11S 球蛋白热聚集的抑制不是由于电荷的作用。     

不同工艺条件对大豆分离蛋白7S和11S组分影响的探讨

利用碱提酸沉的工艺，通过改变温度和离子强度得到不同参数条件下的大豆分离蛋白。经过凝胶电泳分析得到蛋白质的各个条带组分图，用图像捕捉成像技术以及相关软件，分析出分离蛋白各个组分的详细情况（包括组分数、分子量和各个组分所占的百分含量）。由实验可知，分离蛋白的7S和11S组分随温度和离子强度的改变而发生变化，分析其变化规律，从而确定合适的工艺参数。     

等电点附近大豆分离蛋白乳化稳定性的研究

等电点附近的大豆蛋白由于所带电荷减少、疏水相互作用增强而以聚集体的形式存在且其溶解性较差,故鲜有研究者关注该条件下大豆蛋白的乳化特性。本研究从颗粒稳定乳液的角度出发,分别以等电点附近(p H 5.0)和远离等电点(p H 7.0)两个条件制备了大豆分离蛋白(soy protein isolate,SPI)稳定的乳液,比较了两种条件下SPI的界面性质及所得乳液的储藏稳定性。结果发现,p H 5.0时SPI的溶解度仅为4.70±0.15%,远远低于p H 7.0时的93.28±1.89%;然而SPI浓度为0.50%时,p H 5.0的界面压却高于p H 7.0;以p H 5.0条件制备的SPI乳液,其界面蛋白吸附量高达87.03±1.28%,而p H 7.0制备的乳液仅为36.15±1.48%;p H 5.0的乳液两个月后液滴的平均粒径为63.15±0.30μm,与新鲜制备乳液(62.36±0.41μm)相比基本不变;p H 7.0的乳液经过两个月储藏后其液滴平均粒径从45.78±0.38μm增加至55.19±1.86μm。可见,以等电点附近条件制备的SPI乳液依然具有良好的储藏稳定性。     

Survival of Listeria innocua after Isoelectric Solubilization and Precipitation of Fish Protein

ABSTRACT:  Protein wasted by the disposal of fish processing by-products may be recovered using isoelectric solubilization and precipitation. Extreme pH shifts are used to solubilize the protein and then it is recovered by precipitation and centrifugation. Microbial survival after this process is unknown; therefore, the purpose was to see if Listeria innocua would survive extreme pH shifts during the protein recovery process. Fresh rainbow trout fillets were inoculated with L. innocua , homogenized, and brought to the target pH of 2, 3, 11.5, or 12.5 by the addition of concentrated hydrochloric acid or sodium hydroxide. The proteins were allowed to solubilize at 4 °C for 10 min, centrifuged, and the lipid and insoluble components (bones, skin, insoluble protein, and so on) were removed. A 2nd pH shift (pH 5.5) and centrifugation was used to separate the precipitating protein and water fractions. Each constituent (lipid, protein, water, insoluble components) was analyzed for bacterial content using growth and selective media. The sums of the surviving L. innocua in these constituents were compared to the initial inoculum. There were no significant differences in recovery on growth or selective media ( P > 0.05). The greatest loss occurred when the pH was shifted to 2, with a 3.1-log reduction in the combined fractions of the trout fillets and a 3.8-log reduction in the protein fraction. There were no significant losses when the pH was adjusted to 11.5 ( P > 0.05). Future studies will continue to look at the effects of using organic acid, rather than inorganic, for protein solubilization.     

微生物转谷氨酰胺酶催化大豆11S球蛋白聚合研究

研究了微生物转谷氨酰胺酶（MtGase）催化大豆11S球蛋白的聚合反应条件。研究显示，TGase对11S的不同亚基反应不一样，它只能催化11S酸性亚基聚合，而碱性亚基几乎不受影响。离子强度I＝0．1时TGase催化活性要高于I＝0．5，这可能是酶海性受离子强度的影响。酶浓度范围为10－40U/g对TGase催化11S酸性亚基影响不大。TGase催化11S聚合的最适pH为7．0－8．0，pH过高或过低都不利于该酶反应。而在低于50℃范围内，温度越高TGase催化11S聚合越快达到平衡，37℃反应4h与50℃反应2h聚合效果差不多，而60℃已使TGase几利完全失活。     

大豆蛋白11S组分的分离方法研究

采用Nagano法结合电泳图谱ImageMaster 1 D Elite V4.00软件分析法,对大豆分离蛋白的11S组分进行了分离效果研究。确定最佳工艺参数组合为:酸沉pH值6.4、Ca2 浓度40mmol/L和冰浴时间5h。制得的样品中11S组分含量可以达到81.9%。     

Biopolymers Produced by Cross-linking Soybean 11S Globulin with Whey Proteins using Transglutaminase

Heterogeneity of biopolymers was determined by cross-linking acetylated-11S acidic subunits (Ac-11S) of soy protein with α-lactalbumin and β-lactoglobulin. The extent of polymerization was determined by electrophoresis and HPLC. Differential scanning calorimetry (DSC) was used to determine thermal properties of starting proteins and biopolymers. HPLC data demonstrated the absence of biopolymers from Ac-11S, acetylated α-lactalbumin and acetylated β-lactoglobulin when each was incubated separately with transglutaminase (TG). However, Ac-11S formed biopolymers with α-lactalbumin and β-lactoglobulin when TG was added. TG catalyzed the formation of heterologous and homologous biopolymers from whey protein isolate (WPI) and soybean 11S globulin (11S). Cross-linking WPI and 11S provided biopolymers with improved heat stability which may be useful to provide functionality to food products.     

Properties of Biopolymers from Cross-linking Whey Protein Isolate and Soybean 11S Globulin

Biopolymers were prepared by cross-linking whey protein isolate (WPI) and soybean 11S using transglutaminase. Electrophoretic pattern, solubility, emulsification, hydrophobicity and foaming properties of the biopolymers were determined. SDS-PAGE showed bands corresponding to high-molecular-weight components (MW>200 kDa). Biopolymer solubility was > 90% at pH 3 and below, and at pH 7 and above. Emulsifying properties of biopolymers were lower than those of WPI. The foaming capacity of the biopolymers (23.6 mL) and WPI/11S mixture (22.7 mL) were similar to that of egg albumin (20.3 mL). The foaming stability of the biopolymers (122 min) was higher than that of WPI/11S mixture (33.7 min), and was similar to that of egg albumin (132 min).     

大豆7S和11S球蛋白对面团特性及馒头品质的影响

本文研究了大豆浓缩蛋白(CSP)、7S和11S球蛋白的添加对小麦粉面团的粉质、糊化、水分分布、迁移等特性和对馒头质构及感官品质的影响。结果表明:添加CSP可使面团的稳定时间增加,弱化度减小,而添加7S和11S可使面团的稳定时间减小,弱化度增加;添加CSP、7S和11S混合粉面团的抗老化程度、持水性有强到弱依次为11S、7S、CSP;馒头的硬度、咀嚼性均有所降低,由大到小依次为CSP、7S、11S;添加3%的11S球蛋白的馒头形态、质构、口感、风味良好,感官评分最高(90分)。本研究可为CSP、7S和11S在馒头中的应用提供理论依据。