豆源降血压肽制备及活性评价方法的研究进展

食源性降血压肽比目前使用的合成降血压药物毒副作用小,且更易吸收。我国豆类品种丰富、产量高,豆源降血压肽是作为降血压药物的良好选择。介绍了豆源降血压肽的作用机制、制备及活性评价方法,并对常见豆源降血压肽进行综述及展望。     

食品蛋白降血压肽及其研究进展

食品降血压肽已成为生物活性肽研究领域的热点。综述血管紧张素转化酶对血压的调节作用、降血压肽的降血压机理和降血压肽结构与抑制ACE的关系，介绍了食品降血压肽的制备及分离纯化方法。     

食源性降血压肽构效关系与制备研究进展

食物来源降血压肽的研究是近年来在降血压方面的热点研究领域,许多食物蛋白来源的降血压肽经体外实验和动物实验表明具有较强的血管紧张素转化酶抑制活性和显著的降压效果,这为研究开发新型安全高效的降血压产品提供了一条新途径。文章综述了食源性降血压肽的研究进展,重点探讨了以食物为原料制备降血压肽的工艺及降血压肽与结构之间的关系,并对食物源降血压肽的研究应用前景进行了展望。     

降血压肽的研究及应用前景

降血压肽是一种具有降血压作用的蛋白水解产物。文章阐述了降血压肽在降血压方面的作用功能,并对由食品蛋白资源获得的降血压肽的发展趋势、存在问题及应用前景进行了讨论。     

降血压肽的构效关系研究

降血压肽的活性与其氨基酸组成和氨基酸序列有重要的关系.然而,关于降血压肽的构效关系至今尚未清楚.通过对收集的270种降血压肽的氨基酸组成进行分析,研究降血压肽的构效关系以及如何选择蛋白酶和蛋白原料用酶解方法制备降血压肽.结果表明:降血压肽中,N端氨基酸主要为Arg、Tyr、Gly、Val、Ala、Ile和:Leu;C端氨基酸主要为Tyr、Pro、Trp、Phe和Leu;与降血压肽的N端氨基酸特征相比,其C端氨基酸特征对降血压活性影响更为重要.根据降血压肽的构效关系可以看出,在选择蛋白酶和蛋白原料制备降血压肽时,优先选择酶切位点为Tyr、Pro、Trp、Phe和Leu羧基端的蛋白酶以及富含Tyr、Val、Ala、Ile、Leu、Pro、Trp和Phe的蛋白.     

食品蛋白降血压肽及其酶法制备(一)

血管紧张素转换酶在血压调节中扮演重要角色。降血压肽通过抑制血管紧张素Ⅰ向血管紧张素Ⅱ的转化以及阻止ACE使激肽失活而起降血压的作用。利用某些蛋白酶对食品蛋白质的定位水解而可产生具有降血压活性的短肽。降血压肽的分离提取是降血压肽生产的难点所在。综述降血压肽的作用机制及其酶法制备和分离提取的研究进展。     

降血压肽研究现状及其前景分析

降血压肽是血管紧张素转化酶的抑制剂,可通过抑制人体血管紧张素Ⅱ的生成而达到降低血压的目的。降血压肽毒副作用低、降压效果明显、来源广泛,已成为目前研究的热点。本文介绍了降血压肽的研究现状、降血压机理、制备方法及我国降血压肽研究中存在的问题及前景。     

酪蛋白源降血压肽稳定性及其抑制作用机理的研究

酪蛋白源降血压肽经体外胃肠道蛋白酶消化后,其ACE抑制活性仍能保持原来活性的94%.降血压肽与ACE作用前后,其ACE抑制活性和肽谱基本保持不变,证实了酶解乳蛋白源降血压肽是真正的抑制剂类型,不受ACE作用.采用抑制酶解动力学方法,初步探讨降血压肽的抑制作用机理,根据lineweaver-Burk方程,确定酶解酪蛋白源降血压肽是非竞争性抑制类型.     

高活性酪蛋白源降血压肽酶解工艺优化及降血压作用研究

以牛乳来源的酪蛋白为原料,对酪蛋白的酶解工艺进行优化,重点探讨降血压肽的ACE抑制作用,并通过4周的动物实验,对降血压肽的辅助降血压作用进行了初步研究。结果表明,最优水解条件为胰蛋白酶添加量0.4%,酶解温度50℃,pH8.0,底物浓度10%,酶解时间3h;优化工艺制备的降血压肽样品对ACE的IC_(50)为62.4μg/mL,证明降血压肽具有辅助降血压作用。     

植物源降血压肽研究进展

降血压肽的实质是血管紧张素转化酶抑制肽,它通过抑制血管紧张素转化酶(ACE),阻碍有升高血压作用的血管紧张素Ⅱ的生成,同时抑制具有降血压作用的血管舒缓激肽的分解,从而使血压下降。对血压调节机制,降血压肽的结构和组成对其功能的影响,以及目前植物源降血压肽研究进展进行了综述。     

如何提高食源性ACE抑制肽活性的探讨

就如何提高食源性ACE抑制肽的活性，分别对原料、蛋白酶和分离纯化方法等几方面的选择作了探讨。     

ACE抑制肽构效关系研究进展

血管紧张素转化酶(angiotensin-converting enzyme,ACE)抑制肽是一类从食源性蛋白质中分离得到的具有降高血压活性的多肽。由于其降血压效果好,而且没有降压药物的毒副作用从而引起了广泛关注。近年来,ACE抑制肽的构效关系研究成为研究重点。结构生物信息学研究表明,ACE抑制肽的ACE抑制能力不仅与其分子质量有关,而且与其氨基酸序列以及其立体空间构象之间存在高度相关性。ACE抑制肽的抑制类型与ACE抑制活性、构效关系也存在一定相关性。对ACE抑制肽构效关系进行深入研究将有助于指导开发高活性的功能性食品及降血压药物。     

Isolation and Characterization of Peptides with Antihypertensive Activity in Foodstuffs

Hypertension is one of the main causes of cardiovascular diseases. Synthetic drugs inhibiting ACE activity present high effectiveness in the treatment of hypertension but cause undesirable side effects. Unlike these synthetic drugs, antihypertensive peptides do not show any adverse effect. These peptides are naturally present in some foods and since hypertension is closely related to modern diet habits, the interest for this kind of foods is increasing. Different methods for the purification, isolation, and characterization of antihypertensive peptides in foods have been developed. Nevertheless, there is no revision work summarizing and comparing these strategies. In this review, in vivo and in vitro pathways to obtain antihypertensive peptides have been summarized. The ACE mechanism and the methodologies developed to assay the ACE inhibitory activity have also been described. Moreover, a comprehensive overview on the isolation, purification, and identification techniques focusing on the discovery of new antihypertensive peptides with high activity has been included. Finally, it is worthy to highlight that the quantitation of antihypertensive peptides in foods is a new trend since genotype and processing conditions could affect their presence. Analytical methodologies using mass spectrometry constitute an interesting option for this purpose.     

大豆肽的大孔吸附树脂以及凝胶过滤色谱分离

采用DA201．C型大孔吸附树脂对Alcalase水解。DH14％的大豆肽进行脱盐和乙醇分布洗脱，不同浓度乙醇洗脱物的氨基酸组成分析结果表明：洗脱是按照疏水性递增的方式进行的。乙醇浓度为75％时洗脱下来的组分都具有最高的降血压活性，其ACE抑制率为56．52％。体外模拟实验测定结果表明：经过胃肠道酶的作用，大豆肽的ACE抑制活性仍达到49．52％。采用1M的醋酸作为洗脱液可以实现75％乙醇洗脱组分的Sephadex G-15有效分离，其中ACE抑制活性最强组分的抑制率为69．57％．IC50为0．144mg／mL。     

食品蛋白质降血压肽的研究进展

在阐述血管紧张纛转化酶抑制剂降压机理的基础上，综述了食品蛋白质降血肽的研究进展，对结构与活性之间的关系及其在降低高血压患者血压中的重要性进行了讨论，并展望了其广阔的发展前景。     

不同分子量段大豆多肽功能特性的研究

采用Alcalace和Neutrase双酶分步水解法,制备了水解度约为24%的大豆多肽,用截留分子量分别为30000、10000、5000Da的超滤膜将其分离成4个分子量段,对不同分子量段大豆多肽的溶解性、起泡性及起泡稳定性、乳化性及乳化稳定性、抗氧化性和ACE抑制活性进行了研究.     

Identification of an Angiotensin I-converting Enzyme Inhibitory Peptides from Protein Hydrolysates by a Soybean Protease and the Antihypertensive Effects of Hydrolysates in 4 Spontaneously Hypertensive Model Rats

ABSTRACT: Our previous study demonstrated that, because of its substrate specificity, protein hydrolysates by protease D3, which is originated from soybean, exhibited the prominent property of being less bitter than other enzymatic hydrolysates. In the 1st experiment in this series, angiotensin I-converting enzyme (ACE) inhibitory peptides from soy protein hydrolysate by D3 were identified by the establishment of a novel and effective peptide identification method. The amino acid sequences of candidate ACE inhibitory peptides were determined by electrospray ionization mass/mass spectrometry (MS/MS) analysis after rough purification of the samples with gel filtration chromatography and reverse-phase chromatography. Some of the candidate peptides had amino acid sequences that showed homology with those of the reported ACE inhibitory peptides. Then, 8 types of novel candidate peptides were synthesized according to a solid-phase method, and their ACE inhibitory activity was confirmed as the IC₅₀ value. The most potent inhibitor was NWGPLV (IC₅₀= 21 μ M ). In the 2nd experiment, the antihypertensive activity of protein hydrolysates by D3 was investigated in spontaneously hypertensive model rats (SHRs). The dose-dependent antihypertensive effect of soy protein hydrolysate was confirmed, and systolic blood pressure was significantly reduced after the oral administration of doses exceeding 100 mg/kg. Casein hydrolysate was found to have the most potent effects on suppressing blood pressure as well as ACE inhibitory activity among the various food protein hydrolysates studied because of the primary structure of casein. These results indicate that hydrolysates by D3 could be a useful food ingredient because it has the physiological function (antihypertensive activity).     

酶解-膜分离组合制备ACE抑制肽

测试了膜分离操作压力、温度、pH值、料液体积浓度等操作参数对酶活力、血管紧张素转换酶(ACE)抑制肽分离的影响,并建立分段酶解、分级膜分离组合模式实现从扇贝裙边酶解产物中分离ACE抑制肽.结果表明:膜分离操作操作参数对酶活力、ACE抑制肽分离均有较大影响;二段酶解-二级膜分离组合模式制备及分离ACE抑制肽的得率最高,为5.73%,其IC50为0.088mg/ml;一段酶解-二级膜分离组合模式制备及分离ACE抑制肽的得率为3.19%,其IC50为0.081mg/ml;一段酶解-单级膜分离组合模式制备及分离ACE抑制肽的得率只有2.31%,其IC50为0.078mg/ml.     

预处理对胶原蛋白水解和血管紧张素转化酶抑制肽段释放的影响

以胰蛋白酶为工具酶,研究短时热处理、超高压处理对胶原蛋白水解和血管紧张素转化酶(angiotensin converting enzyme,ACE)抑制肽段释放的影响。结果表明:热处理可显著促进胰蛋白酶对胶原蛋白的水解和ACE抑制活性肽段释放,超高压处理组水解物水解度(degree of hydrolysis,DH)与无处理组无显著差异,ACE抑制活性显著低于无处理组。水解物DH和ACE抑制活性关系研究显示,胰蛋白酶水解胶原蛋白过程中,水解度小于5%时,ACE抑制率随水解度呈明显上升趋势,水解度大于5%后,其上升趋势不再明显。肽谱分析进一步证明热处理可有效促进胶原蛋白的水解,超高压处理可改变胰蛋白酶作用位点。热处理组水解物序列分析显示,获得序列均来源于胶原蛋白三螺旋区域,且大部分序列都具有潜在的ACE抑制活性。说明短时热处理可以有效破坏胶原蛋白的三螺旋结构,促进ACE抑制肽段的释放。     

Identification of antioxidant and ACE‐inhibitory peptides in fermented milk

The angiotensin‐converting enzyme (ACE)‐inhibitory activity and antioxidant properties of a commercial fermented milk from Europe were evaluated. This dairy product showed moderate ACE‐inhibitory activity and ABTS^?+ radical‐scavenging capacity. The peptides from most active fractions collected by reverse phase high‐performance liquid chromatography (RP‐HPLC) were sequenced by RP‐HPLC–tandem mass spectrometry. This technique allowed rapid identification of peptides included in the most active fractions, and various potentially active peptides were recognised according to previous studies of structure–activity relationship. Three of the identified sequences had previously been described as potent ACE inhibitors. The structure of some sequences substantiated the presence of peptides with ACE‐inhibitory, antioxidant and immunomodulatory activities. Copyright © 2005 Society of Chemical Industry