酰化作用后菜籽蛋白质的机能和营养价值的评价

将菜籽油用无水琥珀酸进行各种程度的酰化作用变为乙酰化菜籽蛋白浓缩液和丁二酰化菜籽蛋白浓缩液。在本实验中,赖氨酸的8—氨基酸的5％～82％乙酰化菜籽蛋白浓缩液,以及5％～56％的丁二酰化菜籽蛋白浓缩液受酰化作用。在等电点附近,蛋白质的溶解度,乳化力,比粘度由干酰化作用而得以改善。丁二酰基比乙酰基的导入效果大。将丁二酰化菜籽蛋白浓缩液的营养与无修饰菜籽蛋白浓缩液和菜籽粉末相比较,在丁二酰化菜籽蛋白浓缩液中赖氨酸的营养成分的有效性和净电面率减少,菜籽蛋白质浓缩液中的氮消化率也有所减少。     

限制性酶解燕麦蛋白功能特性和抗氧化活性

利用碱性蛋白酶限制性酶解燕麦蛋白,研究了不同水解度(DH)酶解物的溶解性、乳化性、乳化稳定性及对DPPH自由基清除率。试验结果表明,限制性酶解后燕麦蛋白的功能性质有了很大提高。水解初期,随着DH增加,溶解性增大,当DH为15%, pH 8时,溶解度达到79.78%,比原料蛋白在此pH下的溶解性提高了163.91%。乳化性随DH增加而降低,当DH为5%, pH 8时,乳化性达到0.852,比原料蛋白在此pH下的乳化性提高了56.04%。乳化稳定性的变化规律与乳化活性相反,当DH为20%, pH 8时,乳化稳定性达到73.14%,比原料蛋白在此pH下的乳化性提高了59.76%。酶解物对DPPH自由基清除率随着DH增加而变大, DH 5%、DH 10%、DH 15%和DH 20%酶解物对DPPH自由基清除率的IC_(50)分别为6.274, 6.145, 6.050和5.640 mg·mL~(-1),而且浓度与清除率呈现出明显的剂量效应。     

改性对玉米蛋白质功能性质和结构的影响(II)酰化

通过乙酰化和琥珀酰化对玉米蛋白质功能性质和结构的影响研究发现 ,随酰化试剂用量的增大 ,蛋白质的酰化程度提高 ,且在相同摩尔酰化试剂剂量下 ,乙酰化程度高于琥珀酰化 :随酰化程度的增大 ,玉米蛋白质的溶液粘度 ,表面疏水性和分子柔性不断增大 ,蛋白质的等电点向酸性方向漂移 ,水溶性 ,乳化活性和乳化稳定性在等于或高于原蛋白质等电点的pH范围内增大 ,而在低于原蛋白质等电点的pH范围内降低 ;酰化程度越高对蛋白质功能性质和结构的影响越大 ,相同摩尔酰化试剂剂量下 ,琥珀酰化的影响大于乙酰化。     

酰化对大豆蛋白结构和功能性质影响

酰化改性是现代食品蛋白质化学的研究热点。通过对大豆蛋白质乙酰化和琥珀酰化的改 性研究发现,随酰化试剂用量的增大,酰化程度不断提高,在相同酰化试剂用量下,乙酰化 程度高于琥珀酰化。随酰化程度增大,大豆蛋白质表面疏水性,分子柔性和溶性粘度不断 增大,这表明酰化改变了大豆蛋白的结构;在低于原大豆蛋白等电点的ｐＨ范围内,酰化 对其功能性质影响不大,而在高于或等于原大豆蛋白等电点的ｐＨ范围内,酰化可显著地 提高大豆蛋白的水溶性,乳化活性和乳化稳定性,琥珀酰化对大豆蛋白结构和功能性质的 影响均大于乙酰化。研究还发现酰化可使大豆蛋白质的等电点降低。     

水解度对麦胚清蛋白酶解物功能特性和抗氧化力影响

利用碱性蛋白酶限制性酶解麦胚清蛋白,研究不同水解度(degree of hydrolysis,DH)酶解物的溶解性、乳化性等功能特性,及对DPPH自由基和羟自由基清除等抗氧化能力。实验结果表明,水解后清蛋白酶解物的溶解性得到改善,DH越高溶解性越好。DH为8.34%时,等电点处的溶解度从未水解时的49.52%提高到74.09%。而乳化性和乳化稳定性随DH的增加而降低。当DH低于7.54%时,酶解物对DPPH自由基和对羟自由基的清除率随DH的提高而增强。浓度为100 mg/mL,DH为7.54%时的酶解物对DPPH自由基清除率达到59.68%。浓度为5 mg/mL时,DH为7.54%时的酶解物对羟自由基清除率达50.23%。     

不同酶水解菜籽蛋白的水解物的抗氧化活性研究

使用alcalase、protamex、flavourzyme、木瓜蛋白酶、中性蛋白酶和胰蛋白酶共6种蛋白酶水解菜籽蛋白,研究水解物清除DPPH自由基能力、还原能力和抑制亚油酸过氧化活性。结果表明,6种蛋白酶水解菜籽蛋白的水解物都具有抗氧化活性,但水解物的抗氧化活性与水解所用酶的种类和水解时间有关,胰蛋白酶和flavourzyme水解物显示了较强的清除DPPH自由基和还原能力,6种蛋白酶水解物抑制亚油酸过氧化活性高于VE,但略低于BHT。alcalase水解菜籽蛋白时,水解10~45 m in的水解物清除DPPH自由基和还原能力较强,延长水解时间并不能提高其抗氧化活性。     

高压均质对菜籽蛋白功能性质和酶解效果的影响

为了了解高压均质技术对菜籽蛋白的影响,采用不同压力(306、0、901、201、50 MPa)对菜籽蛋白溶液进行均质处理,并分析了处理前后菜籽蛋白功能性质和水解度的变化。结果表明:高压均质可提高菜籽蛋白的溶解度、乳化性、起泡性和泡沫稳定性等功能性质,且随着均质压力的升高其乳化性、起泡性和泡沫稳定性均增强;同时高压均质对蛋白质的氮溶指数、乳化稳定性也有显著的影响;此外,高压均质对菜籽蛋白的酶解也起到了促进作用,且随着压力的增大作用效果越明显。     

碱性蛋白酶水解时间对玉米谷蛋白理化性质及抗氧化活性的影响

为探究碱性蛋白酶(alcalase)水解对玉米谷蛋白理化性质及抗氧化活性的影响,对不同水解时间获得的玉米谷蛋白水解物的表面疏水性、二硫键含量、热性能、分子质量分布、抗氧化活性等进行了评价。结果表明：碱性蛋白酶水解对玉米谷蛋白的性质有显著影响,分子质量和二硫键含量显著降低(P<0.05),与玉米谷蛋白相比其水解物具有较高的溶解性、起泡性、乳化性和热稳定性。此外,玉米谷蛋白水解产物具有良好的抗氧化性能,当水解时间为150 min时玉米谷蛋白水解物的DPPH自由基清除为(54.46±1.43)%,羟自由基(·OH)清除率为(74.06±1.49)%,Fe²⁺螯合力为(86.69±1.35)%。     

提取方法对银杏蛋白功能特性及抗氧化活性的影响

研究水提酸沉法（water extraction and acid precipitation, WEAP）、碱提酸沉法（alkali extraction and acid precipitation, AEAP）和超声辅助碱提酸沉法（ultrasound-assisted alkali extraction and acid precipitation, UA-AEAP）三种方法对银杏蛋白功能特性和抗氧化活性的影响。以溶解度、起泡性、起泡稳定性、乳化性和乳化稳定性为指标,考察不同提取方法对银杏蛋白功能特性的影响;以亚铁离子螯合能力、1,1-二苯基-2-三硝基苯肼（1,1-diphenyl-2-picrylhydrazyl, DPPH）自由基清除能力和羟基自由基清除能力为指标,评价不同提取方法对银杏蛋白抗氧化活性的影响。结果表明,不同提取方法对银杏蛋白得率和溶解度的影响较大,其中UA-AEAP蛋白得率最高,达11.36%±0.10%;在pH2~12范围内,UA-AEAP银杏蛋白的溶解度最高;提取方法显著影响了银杏蛋白的起泡性、泡沫稳定性和乳化性等功能特性（P<0.05）,UA-AEAP蛋白的起泡性、泡沫稳定性和乳化性均优于AEAP和WEAP蛋白,而对乳化稳定性无显著性影响（P>0.05）;提取方法还影响了银杏蛋白的抗氧化活性,银杏蛋白的螯合亚铁离子能力、清除DPPH自由基能力和清除羟基自由基能力的顺序均为:UA-AEAP>WEAP>AEAP。UA-AEAP蛋白得率高、抗氧化能力和功能特性优于另外两种方法,适用于银杏蛋白的制备。     

酶解程度对花生蛋白理化性质及功能特性的影响

研究了不同酶解程度对花生蛋白理化性质(包括分子质量、表面疏水性、巯基含量)及功能特性(溶解性、乳化性、抗氧化性)的影响。研究发现:花生蛋白进行不同酶解处理后,分子质量变小、表面疏水性变小、总巯基及暴露巯基呈现先减小后增大的趋势,同时酶解物的功能性质也发生了较大改变,如所有酶解物的溶解性提高,水解产物的乳化稳定性降低,DH5的乳化活性较PPI强,深度水解后DH10、DH15的乳化活性较PPI均明显下降,多酚含量跟DPPH自由基清除率正相关。研究结果为花生蛋白的改性提供了一定的数据支持。     

Effects of acetylation and succinylation on the functional properties of the canola 12S globulin

The canola 12S globulin was isolated by the protein micellar mass procedure (PMM) and modified by acetylation and succinylation in order to obtain a canola protein concentrate with improved functional properties. The solubility profile differed from that of the PMM in that protein solubility below the isoelectric point was impaired, but solubility at neutral to alkaline pH values was greatly enhanced. In comparison with the PMM foaming capacity and emulsifying activity were significantly increased by acylation. Foam stability decreased significantly upon acylation. Emulsion stability significantly increased initially, then decreased at the highest levels of modification. Following acylation, the fat absorption capacity was significantly elevated. In addition, gelation properties of canola proteins were mainly improved by acylation. Furthermore, the acylated concentrates were significantly lighter in colour than the original PMM. Overall, the acylated concentrates possessed improved functionality as compared to the PMM, making them more suitable as a food ingredient.     

The acylated protein derivatives of Canavalia ensiformis (jack bean): A study of functional characteristics

Protein concentrate was prepared from jack bean (JNP) and it was modified by acylation using acetic (JAP) and succinic anhydrides (JSP). Proximate analyses revealed that moisture and ash content increased following acetylation and succinylation, while both acetylation and succinylation reduced percentage crude fat and protein. Acetylation and succinylation reduced protein solubility in the acidic pH range below the isoelectric point (4.5) of the protein concentrate but improved the solubility of the unmodified protein concentrate at the isoelectric point and pH range alkaline to the isoelectric point. Both acetylation and succinylation increased the water absorption capacity of unmodified protein concentrates at all levels of ionic strength investigated (0.1-1.0 mol/l). Acetylation improved oil absorption capacity whereas the tendency to absorb oil reduced after succinylation. Maximal emulsifying activity of native and modified proteins were obtained at pH 10. Emulsion stability of acylated proteins was higher than those of native proteins in the range of pH 4-10 but lower when the pH was 2. Foam capacity and stability of both native and modified proteins increased with increase in protein concentration. Foam capacity of modified proteins increased progressively with increase in pH from 2 to 10. Also, acylated protein derivatives had improved foam capacity over the native protein except at pH 2. Gelation capacity of both native and modified proteins was maximal at the region of isoelectric point.     

酸枣仁蛋白的不同蛋白酶酶解产物功能特性及抗氧化活性分析

以酸枣仁为原料,采用碱提酸沉法对酸枣仁蛋白进行提取,用三种不同蛋白酶(碱性蛋白酶、中性蛋白酶和木瓜蛋白酶)对酸枣仁蛋白进行酶解,得到三种酶解物,研究不同酸枣仁蛋白酶解物的功能特性和抗氧化活性.结果表明,与酸枣仁蛋白相比,不同酸枣仁蛋白酶解物的溶解性、持油性、起泡性及其稳定性、乳化性及其稳定性均具有不同程度地提高,其中,...     

Effects of succinylation and deamidation on functional properties of oat protein isolate

The effects of two different modification methods (deamidation and succinylation) on the functional properties (solubility, water- and oil-binding capacity, foaming capacity and stability, emulsion activity and stability) of oat protein isolates were evaluated. Protein isolates extracted from defatted oat flour at alkaline pH were acylated by 0.20 g/g of succinic anhydride. The protein isolate was also modified using a mild acidic treatment (HCl, 0.5 N). Succinylation and deamidation improved solubility and emulsifying activity of the native protein isolate. Foaming capacity of oat protein isolate increased after deamidation, whereas succinylation decreased it. The deamidated and succinylated proteins had lower foam and emulsion stabilities than had their native counterpart. Water- and oil-binding capacity, in both modified oat proteins, was higher than those of the native oat protein isolate.     

胞壁蛋白酶（CEP）酶解对酪蛋白结构及功能特性的影响

通过纳米粒度分析、傅立叶红外光谱（FTIR）、乳化性、乳化稳定性、蛋白溶解性、抗氧化性及ACE抑制率的测定,分析探讨酪蛋白及其不同水解度（DH 2.4%、4.5%、7.1%、8.3%）的嗜酸乳杆菌胞壁蛋白酶（CEP）酶解产物的结构及功能特性。FTIR分析表明CEP酶解改变了酪蛋白各种构象所占的比例,酪蛋白二级结构发生了不同程度的变化;纳米粒度分析表明酪蛋白颗粒大小随水解的加深先减小后增大,其水解物颗粒在DH 4.5%时最小,乳化稳定性最大;酪蛋白的乳化性随水解的加深先增大后减小,DH 7.1%时增至最大,与其溶解性的变化趋势一致;此外酪蛋白的酶解物具有一定的ACE抑制活性及抗氧化性,且DPPH清除能力在一定范围内随水解度及浓度的增大而增大,当DH为8.3%,浓度为5mg/mL时,DPPH清除能力增大至35.00%。因此CEP酶解可有效改善酪蛋白的结构及功能特性,为乳源性功能多肽的开发提供理论依据。     

Functional properties of plant proteins. Part 8. Effect of succinylation on some functional properties of the main globulin fraction from rapeseed (Brassica napus L.)

The changes of some functional properties - solubility, emulsifying and foaming properties, heat-induced aggregation - of a native rapeseed globulin preparation after succinylation has been studied. In correspondence with the results obtained with the purified rapeseed 12 S globulin and other globulin preparations from plant seeds, a total blocking of the amino groups of the rapeseed globulin could not be attained. The highest degree of modification reached was 83%. The unmodified protein has high foam capacity and stability. Succinylation until 61% did not change these properties. The emulsifying activity and emulsion stability were slightly improved after a modification at a low or moderate level. The heat-coagulation of the native protein is depressed by increasing succinylation.     

Functional properties of chemically modified proteins of sardine meal defatted with 1-propanol

After extracting oil from sardines using 1-propanol, the proteins of the residual defatted meal were chemically modified using either succinylation, acetylation, maleylation or phosphorylation, and their functional properties were investigated. The solubility and viscosity of defatted meal protein was improved by succinylation and maleylation. The modified proteins had higher emulsifying activity. Succinylated and maleylated proteins had superior emulsifying capacity and emulsion stability. The nutritional qualities of the modified proteins, based on their amino acid compositions, were somewhat decreased. Modification of the electrostatic and hydration characteristics of protein molecules to a more highly charged state by succinylation and maleylation could be effective in improving the functional properties of defatted meal proteins.     

Functional Properties of Acylated Oat Protein

Protein extracted from defatted oat (Avena sativa L., variety Sentinel) was acylated with acetic or succinic anhydride at levels of 0.05 and 0.20 g/g protein. Acetic anhydride was more reactive than succinic anhydride in modifying lysine groups. Total essential amino acid content was slightly lowered by acetylation but unaffected by succinylation. Gel filtration chromatography showed some dissociation of oat polypeptides by succinylation. Solubility, emulsifying properties and fat finding capacity were all markedly improved by acylation, and the effect was more pronounced with succinylation. Emulsifying capacity of meat was enhanced by blending with acylated oat protein. Water hydration capacity and foam stability were adversely affected by acylation. Results suggest that acylated oat protein may be a valuable functional ingredient in meat and other emulsion food products.     

Effects of Acylation on the Functional Properties and In Vitro Trypsin Digestibility of Red Kidney Bean (Phaseolus vulgaris L.) Protein Isolate

ABSTRACT:  The effects of succinylation and acetylation on some functional properties and the  in vitro  trypsin digestibility of kidney bean protein isolate (KPI) were investigated. The extent of succinylation or acetylation progressively increased from 0% to 96% to 97%, as the anhydride-to-protein ratio increased from 0 to 1 g/g. Polyacrylamide gel electrophoresis (PAGE) and zeta potential analyses indicated that acylation, especially succinylation, considerably increased the net charge and hydrodynamic radius of the proteins in KPI, especially vicilin. Acylation treatment at various anhydride-to-protein ratios (0.05 to 1 g/g) remarkably improved the protein solubility (PS) and emulsifying activity index (EAI) at neutral pH, but the improvement by succinylation was much better than that by acetylation. Succinylation resulted in a marked decrease in mechanical moduli of heat-induced gels of KPI, while the mechanical moduli were, on the contrary, increased by acetylation. Additionally,  in vitro  trypsin digestibility was improved by the acylation in an anhydride-type and level-dependent manner. The results suggest that the functional properties of KPI could be modulated by the chemical acylation treatment, using succinic or acetic anhydride at appropriate anhydride-to-protein ratios.