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1.
为了拓宽蚕豆蛋白在食品中的应用,解决传统工业方法制备的蚕豆蛋白溶解性差的问题,本文以传统的碱溶酸沉法提取的蚕豆蛋白为原料,采用限制性酶法对其进行增溶改性工艺优化,并对改性后的蚕豆蛋白的功能性质进行了研究。结果表明:风味蛋白酶是提高蚕豆蛋白溶解性的适宜用酶,酶解改性的最佳工艺条件为:料液比1∶14、酶加量(ES)0.1%、温度58℃、pH值7.5、酶解时间30 min,此条件下蚕豆蛋白的溶解性达到99.73%。改性后的蚕豆蛋白的溶解性、起泡性、乳化性及乳化稳定性在酸性和碱性条件下均显著提高,泡沫稳定性在碱性条件下显著提高,持水力在pH值为2~12的范围内显著下降。  相似文献   

2.
邵平  孙培龙  孟祥河  姜绍通 《核农学报》2007,21(3):268-272,280
对小麦面筋蛋白进行琥珀酰化和蛋白酶复合改性以提高其溶解性及其他特性。对复合改性面筋蛋白与原面筋蛋白、琥珀酰化面筋蛋白、碱性蛋白酶改性面筋蛋白进行了比较。结果表明:在pH 3~11、水解度4%~12%的范围内,复合改性面筋蛋白的溶解度亦随着水解度的增大而增大,比原面筋蛋白、酰化面筋蛋白、中性蛋白酶和碱性蛋白酶的改性产物都高。起泡性和起泡稳定性则先增加后降低,在水解度4%时具有较佳值,但在各水解度下较单一改性的面筋蛋白产物都要低。添加复合改性面筋蛋白面团黏弹性和面包口感较好,内部结构均匀、细腻。  相似文献   

3.
为提高酸性条件下大豆分离蛋白（soy protein isolates,SPI）的乳化性能,该文研究了物理-酶联合改性对SPI（pH值为4）的乳化性能影响,通过对比确定了物理-酶联合改性,即超声波-酶复合改性和挤压膨化-酶复合改性两种改性方法在酸性条件下的乳化性能效果最好;并通过对改性后 SPI（pH 值为4）进行溶解性、游离巯基、二硫键、粒径、扫描电镜（scanning electron microscope,SEM）和激光共焦扫描显微镜（confocal laser scanning microscopy,CLSM）分析,从蛋白结构变化上进一步揭示了乳化性能提高现象的原因。结果表明：超声波联合植酸酶-酸性蛋白酶改性的 SPI （Uphy-aci-SPI）的乳化活性（emulsifying activity index,EAI）为0.53 m2/g,比未改性SPI（0.18 m2/g）显著提高了196%（P<0.05）,乳化稳定性（emulsifying stability index,ESI）为17 min,比未改性SPI（13.5 min）显著提高了25.9%（P<0.05）;挤压膨化联合菠萝蛋白酶改性的SPI（Ebro-SPI）的EAI为0.46 m2/g,比未改性SPI显著增加了155%（P<0.05）,ESI为17 min,比未改性SPI显著增加了25.9%（P<0.05）。在pH值为4的条件下对物理-酶联合改性的SPI的性质分析发现,物理-酶联合改性的SPI与未改性SPI相比,物理-酶联合改性的SPI的溶解性显著增加（P<0.05）;物理-酶联合改性的SPI的乳状液平均粒径减小,CLSM观察乳状液中油与蛋白溶液稳定共融,改善了油滴之间的空间排斥力。物理-酶联合改性的SPI游离巯基的含量显著增加（P<0.05）,二硫键含量显著降低（P<0.05）。SEM观察物理-酶联合改性的SPI为结构松散、破碎均一的微观结构。由此可见,乳化性能的提高是通过深层改变蛋白的结构来实现的。该研究可为探索提高酸性条件下SPI的乳化性能的方法提供理论依据。  相似文献   

4.
玉米挤压淀粉酶法改性制膜的工艺优化   总被引：1，自引：0，他引：1  
为了提高可降解性玉米淀粉膜的力学性能,并获得玉米挤压淀粉酶法改性制膜的最适工艺参数,该研究以普鲁兰酶为酶制剂来改善玉米挤压淀粉膜,以酶作用温度、pH值、酶添加量、酶解时间及玉米挤压淀粉浓度为试验因子,膜的抗拉强度为响应值,采用中心旋转组合试验设计进行试验。结果表明：5个因素对酶改性挤压淀粉膜抗拉强度的影响大小依次为玉米挤压淀粉浓度＞酶添加量＞酶解时间＞pH值＞酶作用温度;最佳酶解制膜工艺条件为：酶作用温度46.57℃,pH值4.44,酶添加量6.63 u/g,酶解时间9.31 h,玉米挤压淀粉浓度7.00%,在此条件下,膜抗拉强度的预测值为24.3654 MPa,验证试验所得膜抗拉强度为24.2539 MPa,比未改性膜的抗拉强度提高了338.01%。回归方程的预测值和试验值差异不显著,所得回归模型拟合情况良好,达到设计要求。膜的抗拉强度与酶解挤压淀粉中直链淀粉含量之间存在极显著正相关关系,相关系数为0.863。  相似文献   

5.
为探究牛血加工利用新技术,提高牛血蛋白资源利用率。该研究采用分步酶解法提取牛血红蛋白的抗氧化肽粗提物,从6种蛋白酶中筛选出最适蛋白酶组合,通过单因素试验优化温度、pH值、料液比、酶添加量和酶解时间,并通过响应面设计进一步优化酶添加量和酶解时间,得到牛血红蛋白抗氧化肽粗提物的最佳酶解工艺。结果表明：牛血红蛋白分步酶解的最佳工艺为：料液比40 g/L,一次酶解：风味蛋白酶添加量3 800 U/g、时间130 min、温度50 ℃、pH值7.5;二次酶解：碱性蛋白酶添加量2 900 U/g、时间60 min、温度40 ℃、pH值9.0。此工艺条件下的牛血红蛋白抗氧化肽粗提物的ABTS自由基清除能力为（333.62±6.29）μmol /g,具有优良的抗氧化活性,可作为食源性抗氧化肽的来源。该研究为牛血等副产物的综合加工利用提供了新思路,同时为食源性抗氧化肽的研发提供理论基础。  相似文献   

6.
酶解牛乳蛋白多肽复合果汁乳酒工艺研究   总被引：1，自引：1，他引：1  
为克服传统乳酒缺陷，该文采用蛋白酶水解法及酒精酵母乳酸菌混合发酵法研究了牛乳蛋白多肽复合果汁乳酒的生产工艺。通过对比和正交试验确定了牛乳蛋白的最佳水解酶、水解条件及牛乳蛋白多肽复合果汁乳酒的发酵条件和配方。结果表明：牛乳蛋白的最佳水解酶是中性蛋白酶，最佳水解条件是：酶用量140 mg/L，温度50℃，pH 6.5，酶解5 h,牛乳蛋白水解最彻底；牛乳蛋白多肽复合果汁乳酒的最佳发酵条件为经中性蛋白酶水解的牛乳，用蔗糖调整其糖度为15%，再配以4%的猕猴桃浓缩汁，添加0.35％ kefir发酵剂在25℃发酵12 h，发酵液中的酒精及总酸含量较高；牛乳蛋白多肽复合果汁乳酒的最佳配方组成是：发酵液60%、糖6%、酸0.28%、甜味剂0.1%、稳定剂0.5%、复合香精0.06%、风味增强剂8 mg/L，乳酒品质最好。  相似文献   

7.
大米蛋白的酶水解动力学研究   总被引：2，自引：0，他引：2  
以米渣为材料,研究碱性蛋白酶、1398中性蛋白酶和木瓜蛋白酶在不同起始pH值、加酶量和温度下水解大米蛋白的进程,建立大米蛋白酶水解动力学方程,为大米蛋白酶水解特性的研究提供依据.在一级化学反应动力学方程基础上,建立了考虑温度、起始pH值和加酶量影响的大米蛋白酶水解动力学模型,该模型可较好的描述不同蛋白酶对大米蛋白的水解进程.木瓜蛋白酶适于在较低的起始pH值下水解,加酶量、起始pH值对其水解进程的影响较大,温度变化对其水解进程的影响较小.1398中性蛋白酶适于在中性条件下水解,加酶量和水解温度对其水解进程的影响程度处于木瓜蛋白酶和碱性蛋白酶之间,起始pH值变化对其水解进程的影响不大.碱性蛋白酶适于在较高pH值下水解,加酶量对其水解进程影响不大,温度的变化对水解进程影响较大.  相似文献   

8.
黑豆蛋白肽果汁复合饮料的研制   总被引：5，自引：1，他引：5  
黑豆是种皮为黑色的大豆，其蛋白质含量高达50%，是极具开发潜力的植物蛋白资源，但黑豆蛋白质分子高度压缩折叠、不易消化，使其加工利用受到了限制。该试验采用2709碱性蛋白酶对黑豆蛋白进行有控制的水解，制备酸溶性好、易消化吸收的黑豆蛋白肽，经水解度与酸溶性蛋白肽得率测定，确定了酶解工艺条件：底物浓度为每100 mL黑豆浆含3.75 g蛋白质，酶-底物比为8 000 u/g，pH值9.0，温度50℃，酶解时间2.0 h，水解度为10%，酸溶性蛋白肽得率达85%。2709蛋白酶对黑豆蛋白具有较好的水解效果，1 kg黑豆经磨浆、酶解与离心去渣脱苦制得20 L黑豆蛋白肽混合液，将其与天然澄清苹果汁按80∶20(V/V)混合调配制备黑豆蛋白肽果汁复合饮料，产品色泽棕红清亮，具天然果汁与黑豆清香风味，蛋白质与肽类物质含量(m/V)≥1.5%，酸度(以柠檬酸计) ≥0.4 g/100 mL。  相似文献   

9.
鲤鱼酶解发酵制饮料的技术研究   总被引：6，自引：0，他引：6  
该文对鲤鱼酶解发酵制饮料的加工技术进行了研究。结果表明：枯草杆菌蛋白酶酶解鲤鱼蛋白的最佳酶解条件是酶用量(酶与底物浓度比，E/S)0.12 g/kg，温度45℃，pH值8.0,在此条件下酶解鲤鱼4 h，氨基态氮含量由0.0017 g/L增加到0.0414 g/L，增加了23倍；游离氨基酸由19.943 mg/(100 mL)增加到78.001 mg/(100 mL)，增加了291%。经保加利亚乳杆菌和嗜热链球菌发酵后，酶解液风味得到明显改善，并产生了特殊的乳酸发酵香味。鲤鱼高压水煮液体外·OH清除率为0.97％，经枯草杆菌蛋白酶酶解后酶解液体外·OH清除率为80.21％，酶解发酵液体外·OH清除率为78.74％。鲤鱼蛋白经酶解和发酵后体外·OH清除能力都得到明显的提高。鲤鱼饮料的配方组成是：鲤鱼酶解发酵过滤液80 g/kg，麦芽糖30 g/kg，蔗糖45 g/kg，乳化稳定剂3 g/kg，浓缩苹果汁15 g/kg，酸味剂和香精适量。  相似文献   

10.
Alcalase酶水解花生蛋白制备花生短肽的研究   总被引：1，自引：2，他引：1  
对Alcalase水解花生蛋白制备花生短肽过程中，酶用量、底物浓度、pH值、反应温度、反应时间等影响因素进行了系统地研究，建立了短肽得率及水解度与各种影响因素的回归模型；在此基础上，结合实际生产确定出了Alcalase酶解花生蛋白的最适条件为pH值8.0，水解温度54℃，底物浓度4%，酶用量3480 U/g，水解时间106 min。在此条件作用下，体系中短肽得率为79.08%，水解度为17.08%，短肽平均链长为5.85，平均分子量为661.5。  相似文献   

11.
The unfolding of beta-lactoglobulin during high-pressure treatment and its refolding after decompression were studied by 1H NMR and 2H/1H exchange at pH 6.8 and 2.5 and at 37 and 25 degrees C. The extent of unfolding increased with the pressure level. The structure of beta-lactoglobulin required higher pressures to unfold at pH 2.5 than at pH 6.8. More flexibility was achieved at 37 degrees C than at 25 degrees C. Results indicated that the structural region formed by strands F, G, and H was more resistant to unfold under acidic and neutral conditions. The exposure of Trp19 at an earlier time, as compared to other protein regions, supports the formation of a swollen structural state at pH 2.5. Refolding was achieved faster when beta-lactoglobulin was subjected to 200 MPa than to 400 MPa, to 37 degrees C than to 25 degrees C, and to acidic than to neutral pH. After treatment at 400 MPa for 20 min at neutral pH, the protein native structure was not recovered. All samples at acidic pH showed that the protein quickly regained its structure. Hydrolysis of beta-lactoglobulin by pepsin and chymotrypsin could be related to pressure-induced changes in the structure of the protein. Compared to the behavior of the protein at atmospheric pressure, no increased proteolysis was found in samples with no increased flexibility (100 MPa, 37 degrees C, pH 2.5). Slightly flexible structures were associated with significantly increased proteolysis (100 MPa, 37 degrees C, pH 6.8; 200 MPa, 37 degrees C, pH 2.5). Highly flexible structures were associated with very fast proteolysis (>or=200 MPa, 37 degrees C, pH 6.8; >or=300 MPa, 37 degrees C, pH 2.5). Proteolysis of prepressurized samples improved only when the protein was significantly changed after the pressure treatment (400 MPa, 25 degrees C, 20 min, pH 6.8).  相似文献   

12.
The properties of whey protein isolate (WPI) stabilized oil-in-water (O/W) nanoemulsions (d(43) ≈ 66 nm; 0.5% oil, 0.9% WPI) and emulsions (d(43) ≈ 325 nm; 0.5% oil, 0.045% WPI) were compared. Emulsions were prepared by high-pressure homogenization, while nanoemulsions were prepared by high-pressure homogenization and solvent (ethyl acetate) evaporation. The effects of pH, ionic strength (0-500 mM NaCl), thermal treatment (30-90 °C), and freezing/thawing on the stability and properties of the nanoemulsions and emulsions were compared. In general, nanoemulsions had better stability to droplet aggregation and creaming than emulsions. The nanoemulsions were unstable to droplet flocculation near the isoelectric point of WPI but remained stable at higher or lower pH values. In addition, the nanoemulsions were stable to salt addition, thermal treatment, and freezing/thawing (pH 7). Lipid oxidation was faster in nanoemulsions than emulsions, which was attributed to the increased surface area. Lipase digestibility of lipids was slower in nanoemulsions than emulsions, which was attributed to changes in interfacial structure and protein content. These results have important consequences for the design and utilization of food-grade nanoemulsions.  相似文献   

13.
The stability of emulsions prepared with soy protein isolates was investigated as a function of pH in the presence of two negatively charged polysaccharides: high methoxyl pectin (HMP) and soy soluble polysaccharide (SSPS). Both polysaccharides are composed of a backbone which contains galacturonic acid but, when added to soy protein isolate-stabilized emulsions, SSPS showed a different behavior than that of HMP. At neutral pH and above a critical concentration of stabilizer (0.05%), HMP caused flocculation of the emulsion droplets via a depletion mechanism. On the other hand, the emulsions containing a similar amount of SSPS did not show creaming or flocculation. At acidic pH (<4.0) the addition of pectin caused extensive droplet aggregation, while no aggregation was observed with the addition of SSPS. The differences in the stabilization behavior between the two polysaccharides can be attributed to their differences in charge, neutral sugars side chains, and molecular weight.  相似文献   

14.
Some nutritional and functional properties of defatted wheat germ protein   总被引：24，自引：0，他引：24  
Defatted wheat germ protein (DWGP) was isolated by alkaline extraction at pH 9.5 and subsequent isoelectric precipitation at pH 4.0, and its nutritional and functional properties were studied. The results showed that the amino acid content of defatted wheat germ was as high as 26.793 g/100 g, and the contents of eight essential amino acids were all relatively high. The isoelectric point of DWGP was 4.0. When pH >6.0, the DWGP had high solubility with a nitrogen solubility index of 70%. The emulsifying activity and emulsifying stability of DWGP were similar to those of bovine serum albumin and a little higher than those of casein. DWGP had good foaming capacity, but its foaming stability (FS) was not very good. However, the FS of DWGP can be improved through physical, chemical, or enzymatic methods. Moreover, DWGP had excellent water retention (WR); especially at pH 8.0 and a temperature of 70 degrees C, the WR of DWGP was the highest at 229.4%. DWGP offers is a potential source of functional protein isolate for possible food applications.  相似文献   

15.
刘蕾  袁芳  高彦祥 《农业工程学报》2016,32(Z2):423-429
为了提高β-胡萝卜素乳液稳定性,该研究利用α-乳白蛋白(α-LA)为乳化剂,考察了不同α-LA添加量(0.25%~3.00%)对10%的水包油(O/W)β-胡萝卜素乳液粒径、电位、快速稳定性、包埋率、界面α-LA含量和化学稳定性的影响。结果表明:随着α-LA添加量的增加,β-胡萝卜素乳液粒径减小,电位增加,包埋率提高;当α-LA添加量大于1.50%时,乳液粒径、电位和包埋率不再随着α-LA添加量的增加而变化(P0.05)。乳液的Turbiscan扫描指数(TSI)在α-LA添加量大于1.50%之后没有显著性变化,β-胡萝卜素乳液趋于稳定。随着α-LA添加量的增加,水油界面上α-LA含量显著增加(P0.05)。当α-LA添加量大于1.00%时,β-胡萝卜素在乳液中的保留率不再随着α-LA添加量的增加而增加。研究结果表明α-LA是一种可以应用在β-胡萝卜素乳液中的乳化剂,在α-LA添加量为1.50%时,可以得到物理和化学稳定性较好的β-胡萝卜素乳液,为食品工业中应用β-胡萝卜素提供了参考。  相似文献   

16.
Soybean proteins have shown great potential for applications as renewable and environmentally friendly adhesives. The objective of this work was to study physicochemical and adhesion properties of soy glycinin subunits. Soybean glycinin was extracted from soybean flour and then fractionated into acidic and basic subunits with an estimated purity of 90 and 85%, respectively. Amino acid composition of glycinin subunits was determined. The high hydrophobic amino acid content is a major contributor to the solubility behavior and water resistance of the basic subunits. Acidic subunits and glycinin had similar solubility profiles, showing more than 80% solubility at pH 2.0-4.0 or 6.5-12.0, whereas basic subunits had considerably lower solubility with the minimum at pH 4.5-8.0. Thermal analysis using a differential scanning calorimeter suggested that basic subunits form new oligomeric structures with higher thermal stability than glycinin but no highly ordered structures present in isolated acidic subunits. The wet strength of basic subunits was 160% more than that of acidic subunits prepared at their respective isoelectric points (pI) and cured at 130 degrees C. Both pH and the curing temperature significantly affected adhesive performance. High-adhesion water resistance was usually observed for adhesives from protein prepared at their pI values and cured at elevated temperatures. Basic subunits are responsible for the water resistance of glycinin and are a good starting material for the development of water-resistant adhesives.  相似文献   

17.
In this study, a protein isolate with a high solubility at neutral pH was prepared from industrial potato juice by precipitation at pH 5 in the presence of ethanol. The effects of ethanol itself and the effects of its presence during precipitation on the properties of various potato protein fractions were examined. The presence of ethanol significantly reduced the denaturation temperature of potato proteins, indicating that the preparation of this potato protein isolate should be performed at low temperature in order to retain a high solubility. In the presence of ethanol, the thermal unfolding of the tertiary and the secondary structure of patatin was shown to be almost completely independent. Even at 4 degrees C, precipitation of potato proteins in the presence of ethanol induced significant conformational changes. These changes did, however, only result in minor changes in the solubility of the potato protein fractions as a function of pH and heat treatment temperature.  相似文献   

18.
We studied gliadin solubility, surface tension and foam behavior, and the presence of different gliadin types in gliadin aqueous solutions and foams as a function of pH. Gliadin has excellent foaming properties only at neutral and alkaline pH. Its solubility is minimal near neutral pH, while almost complete at acidic and alkaline pH. Surface tensions of gliadin solutions are minimal around neutral pH, higher at alkaline pH, and highest at acidic pH, which corresponds well with their respective foaming properties. Foams at acidic and alkaline pH values are enriched in γ-gliadin, while foams at pH 8.0 have a similar distribution of α- and γ-gliadins. Thus, γ-gliadin predominantly contributes to the foaming properties of gliadin. The poor foaming properties of gliadin at pH 2.0 improve in the presence of 0.25 and 1.0% NaCl. It follows that the presence of positively charged amino acid residues hinders the formation of stable foam at acidic pH.  相似文献   

19.
The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 degrees C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.  相似文献   

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