食源蛋白制备血管紧张素抑制肽的研究进展

血管紧张素转化酶(angiotensin I converting enzyme,简称ACE)对于人体血压的调节有着十分重要的作用。血管紧张素转化酶抑制肽(ACEIP)是从食源性蛋白质中提取的功能性肽,有着抑制ACE的作用,从而降低人体血压,达到治疗高血压的目的。本文主要从ACE抑制肽的降压原理、来源、结构、分类及作用特点和前景展望这几方面对其进行总结阐述。     

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。     

食源性血管紧张素转化酶抑制肽的研究进展

食源性血管紧张素转化酶抑制肽是源于食物蛋白的生物活性小肽,它通过抑制生物体内ACE的活性而发挥出显著的降血压效果,并具有安全性高、无副作用、降压效果温和专一等优点,已成为目前国内外的研究热点。主要从食源性ACE抑制肽的降压机理、ACE抑制肽的定性/定量构效关系、肽的活性与降血压的关系等方面进行了详细综述和归纳。     

血管紧张素转化酶抑制肽稳定性研究

高血压是心血管疾病最重要的且可治疗的危险因素之一,控制高血压是降低心脑血管疾病的发病率、致残率和死亡率的有效措施。血管紧张素转化酶通过影响肾素-血管紧张素系统和激肽释放酶-激肽系统实现对人体血压调节。文章综述了血管紧张素转化酶抑制肽的总体研究趋势、物理化学及酶稳定性的研究现状,并对其值得进一步研究内容进行展望,旨在为血管紧张素转化酶抑制肽的研究与开发提供思路。     

蛋清蛋白质降压肽的化学及酶稳定性研究

以血管紧张素转化酶抑制活性为指标,通过Plackett-Burman 设计研究影响蛋清蛋白质降压肽化学稳定性的因素,同时考察蛋清蛋白质降压肽在模拟胃肠道环境中的抗胃蛋白酶和胰蛋白酶裂解的稳定性。结果表明：pH值、温度、光照、空气、贮藏肽溶液的质量浓度、巴氏灭菌处理、超声波及镁离子等因素对蛋清蛋白质降压肽的化学稳定性影响不显著(P ＞ 0.05);蛋清蛋白质降压肽经胃蛋白酶和胰蛋白酶水解后活性由46.0% 分别下降为13.0% 和4.0%,对胃蛋白酶和胰蛋白酶均没有良好的耐受性。     

用玉米大豆复配蛋白制备降血压肽水解酶筛选研究

为了综合利用玉米、大豆加工副产品，使其营养价值、生物活性提高，用三种酶酶法改性复配蛋白质后，采用试剂盒测定了酶解肽抑制血管紧张素Ⅰ转化酶（ACE）的活性，并用HPLC分析了原料中氨基酸的组成。结果表明：复配蛋白质适合用作生产抑制ACE活性肽的原料；中性蛋白酶是一种用于玉米、大豆蛋白制备降血压肽的较理想的酶，当[E]／[S]为0．5％，料液比为1：15，水解时间为3h时，肽的ACE抑制率最高可达99％。     

降血压肽的生理活性及应用

来源于食物蛋白的降血压肽对血管紧张素转化酶（ACE）的活性具有抑制作用。本介绍降血压肽的作用机制,生理效果,研究进展并展望其应用前景 。     

ACE抑制肽的制备及其结构对活性的影响

血管紧张素转化酶（ACE）通过一系列的生理反应,从而起到升高血压的作用,在人体中过量ACE的产生会引起高血压,而生物活性物质ACE抑制肽能够抑制ACE的功能。文章主要综述了ACE抑制肽的主要制备方法及氨基酸序列特点与ACE抑制活性的关系,并阐述了脯氨酸对ACE抑制活性的影响,以及部分氨基酸的结构特点及功能,为今后ACE抑制肽的制备与应用提供参考依据。     

蛋清蛋白源血管紧张素转化酶抑制肽研究进展

在分析蛋清蛋白的组成及酶解性质的基础上,综述了国外蛋清血管紧张素转化酶抑制肽来源、制备方法、降压活性、酶解动力学、结构修饰和包埋技术的研究现状,并对其在食品、医药领域研究和应用的方向进行了展望。以期为我国蛋清蛋白降压肽的研究与开发提供参考。     

血管紧张素转化酶抑制二肽抑制ACE作用的柔性分子对接

食源性血管紧张素转化酶（angiotensin Ⅰ-converting enzyme,ACE）抑制肽可有效抑制生物体内ACE活性,进而起到降压疗效,且作用温和,无副作用,是高血压治疗的理想药物,但其分子作用机制一直未有明确解释。本实验选取4 个代表性食源ACE抑制二肽（Gly-Phe、Gly-Tyr、Val-Phe、Ile-Tyr）为研究对象,采用柔性分子对接的方法研究它们与ACE的相互作用模型与分子机理。分子对接结果表明：氢键、亲水、疏水、静电等作用力同时对二肽与ACE的结合有贡献,但以氢键作用为主;ACE分子中Ala354、Glu384、Arg522等氨基酸残基为二肽与其结合的重要活性位点;ACE抑制二肽中氮端氨基对其抑制活性影响显著。通过以上分子机理研究可为指导开发强活性ACE抑制肽提供理论指导。     

食品蛋白质降血压肽(ACEIP)的开发研究

降血压肽(ACEIP)主要来源于食品蛋白质，其制备过程包括蛋白质的提取、酶水解、降血压肽的分离、脱苦、干燥、检测等环节。介绍和分析了蛋白酶及其酶解条件的选择、活性肽的分离、苦味的脱除及活性的测定等开发降血压肽的关键技术和难点。     

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。     

血管紧张素转换酶抑制剂特性及其分类比较

讨论了ACE酶在血压调节中的生理意义，ACEI的不良反应和ACEIP的特点，不同食物蛋白来源的ACEIP，及这些肽在开发防治高血压的新型功能型食品方面的应用前景。     

Bioactive peptides as natural antioxidants in food products – A review

BackgroundDiseases related to oxidative stress and food quality decay are of major concern worldwide as they can lead to economic losses in both public health and food production. The antioxidant peptides, extracted from food proteins, can be explored as natural new drug and food ingredient.Scope and approachAntioxidant peptides are extracted from non-antioxidant precursor proteins from different origin by the activity of either proteolytic microorganisms or isolated enzymes. In the present review, the main sources of bioactive peptides will be discussed. Moreover, the current strategies to obtain these compounds as well as their health benefits and in vivo biological effects will be evaluated. Considerations for further research and development of strategies to increase the knowledge about this underexplored activity of peptides will be also considered.Key findings and conclusionsBioactive peptides' content and profile differ according to the matrix studied and the method used. The utilization of fermentation processes and enzymes has been established to obtain antioxidant bioactive peptides from proteins, being isolated enzymes the most commonly used method, due to their superior control over releasing and obtaining targeted peptides. Antioxidant peptides have the ability to reduce the formation of oxidative products along with the induction of antioxidant enzymes in vivo. However, at this stage of development more in vivo studies are needed in order to evaluate the specific effects on the health of selected antioxidant peptides. In food technology, successful application in meat products strengthens the role of selected peptides as antioxidant additives, although there is a need to observe the effects of the isolated bioactive peptides in other food matrices along with studies to scale-up its production.     

QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides

An increasing prevalence of hypertension in the world implies the necessity of further study of antihypertensive peptides as an alternative means for hypertension management. The purpose of this study was to evaluate systematically the potential of major food proteins as precursors of ACE inhibitory peptides using QSAR-aided in silico approach, and thus to establish the rationale for choosing the appropriate substrate proteins in preparing ACE inhibitory peptides. In silico digestion of proteins from 15 common food commodities by thermolysin generated 5709 peptides ranging from 2 to 6 amino acid residues. Peptides were divided into three categories based on the potency of their predicted activities. Our results showed that meat proteins from pork, beef and chicken contain the largest number of potent peptides (IC₅₀ < 10 ??M), followed by proteins from milk, egg, soybean and canola, whereas proteins from fish (with the exception of salmon) and cereals (oat and barley) contain the least number of potent peptides. This study demonstrated that proteins from livestock meat, milk, egg, soybean and canola are good sources of ACE inhibitory peptides.     

食物致敏原表位定位技术的研究进展

食物致敏原是引起食物过敏的元凶，多为蛋白质。抗原表位是在抗原分子中与抗体反应或被抗原受体识别，并引发机体免疫应答的特殊化学基团。从表位水平认识食物致敏原，能揭示食物过敏的物质基础，为解决食物过敏问题提供精准的靶标。本文基于表位结构和定位方法的不同，介绍了食物致敏原表位定位技术的发展，并进一步展望了致敏原表位信息对于改进食物过敏鉴定技术和低致敏食物加工方法的应用前景。     

Enzymatic hydrolysis of blue whiting (Micromesistius poutassou); functional and bioactive properties

Functional and biochemical properties of fish protein hydrolysates (FPH) from blue whiting (BW) were studied. FPH (2.5%, 5%, 10%, and 15% degree of hydrolysis [DH]) were made from isolated proteins from headed and gutted BW with Alcalase 2.4 L. The properties of dried BW mince and protein isolate compared to 4 reference proteins (soy and milk protein) were studied: color, solubility, water-holding capacity (WHC), oil-binding capacity (OBC), emulsion capacity (EC), and emulsion stability (ES). The angiotensin I-converting enzyme (ACE) inhibitory activities of the soluble fraction of BW powders were also investigated. Furthermore, the products were characterized by analyzing their chemical composition. Chemical composition, solubility, OBC, and EC of the BW powders was significantly (P < 0.05) different with different DH, while color, ES, and WHC were not significantly (P > 0.05) different. Salt content of the FPH was high (4% to 19%) and increased with increased DH. Protein solubility varied from 10% to 70% and increased with increased DH. WHC of the FPH was around 97% and was higher than that of all the reference proteins tested. OBC decreased with increased DH (from 3.5 to 2.1 g oil/g protein) and was higher than OBC of the soy and milk proteins (1.6 to 1.9 g oil/g protein). EC of FPH was similar or lower than the reference proteins. ES of FPH (60% to 90%) was similar to or lower than soy and whey proteins (60% to 98%) but higher than casein (20%). ACE inhibition activity increased as DH was increased. Practical Application: The results from this study demonstrate that a functional bioactive hydrolysate can be produced from BW, which is an underutilized fish species, and may aid the industry in better utilizing this raw material. The novelty of this research was the use of BW as a raw material where the protein has been isolated with the pH shift method. Furthermore, it was novel that bioactivity and functionality was measured in the same samples.     

Comparative structural, emulsifying, and biological properties of 2 major canola proteins, cruciferin and napin

ABSTRACT:  Canola is an economically important farm-gate crop in Canada. To further explore the potential of canola protein as value-added food and nutraceutical ingredients, a better understanding of fundamental properties of 2 major canola proteins is necessary. Two major protein components, cruciferin and napin, were isolated from defatted canola meal by Sephacryl S-300 gel filtration chromatography. SDS-PAGE showed that cruciferin consists of more than 10 polypeptides, and noncovalent links are more important than disulphide bonds in stabilizing the structural conformation. Napin consists of 2 polypeptides and is stabilized primarily by disulphide bonds. Purified cruciferin showed 1 major endothermic peak at 91 °C compared with that of 110 °C for napin. Emulsion prepared by cruciferin showed significant higher specific surface area and lower particle size than that of napin. The study indicated that the presence of napin could detrimentally affect the emulsion stability of canola protein isolates. Hydrolysates from cruciferin and napin showed potent angiotensin I-converting enzyme inhibitory activity (IC₅₀: 0.035 and 0.029 mg/mL, respectively), but weaker than that of canola protein isolate hydrolysate (IC₅₀: 0.015 mg/mL).     

Emulsifying Properties of Proteins Isolated from Various Rice Cultivars

The emulsifying properties of rice proteins isolated from various non-waxy and waxy rice cultivars were studied to evaluate their potential application as oil-in-water (O/W) emulsifier and to compare the emulsifying properties of the rice proteins isolated from various rice cultivars. The solubility of the rice proteins was measured at different pHs (2–10), and O/W emulsions were prepared with the proteins at pH 2, 7, and 10. The rice protein-stabilized O/W emulsions were analyzed by measurement of particle size and zeta-potential, and observation under an optical microscope. The results indicated the potential of the rice proteins as emulsifiers at low and high pH values, and that, in particular, rice proteins isolated from waxy-rice cultivars could form stable emulsions even at neutral pH. The information obtained in this study may be useful for development of emulsion-based food products using rice protein isolate.