葵花籽ACE抑制肽的微胶囊制备工艺研究

以β-环糊精为壁材研究了葵花籽ACE抑制肽的微胶囊制备工艺及参数。试验结果表明最佳工艺参数:芯壁质量比(葵花籽ACE抑制肽∶β-环糊精)1∶18,包合温度30℃,超声功率150 W,超声时间70 min,在此条件下微胶囊的载药量为4.9%±0.5%。在模拟胃液和肠液中的体外释放实验表明微胶囊化对葵花籽ACE抑制肽起到了一定的缓释效果,且抑制肽活性保持良好,敞口贮藏8 d后ACE抑制率仍可达到29.2%。     

葵花籽ACE抑制肽的体内降压活性初步研究

以自发性高血压大鼠(SHR)建立试验模型,探讨葵花籽ACE抑制肽的体内降压活性。试验结果表明:一次性给药后,葵花籽ACE抑制肽各剂量组对SHR收缩压的降低作用存在明显的量效关系,且降压活性具有时效性;长期灌胃葵花籽ACE抑制肽,SHR体重均呈增加趋势,空白组增加最大,阳性对照组增加最小;在为期4周的长期给药实验中,除低剂量组和空白组的收缩压无显著差异外,其余各组均与对照组相比有显著的差异;各试验组SHR的心率值之间无显著差异性,表明葵花籽ACE抑制肽对SHR心率无显著的副作用。     

葵花籽ACE抑制肽的体内降压活性初步研究

以自发性高血压大鼠(SHR)建立试验模型,探讨葵花籽ACE抑制肽的体内降压活性。试验结果表明:一次性给药后,葵花籽ACE抑制肽各剂量组对SHR收缩压的降低作用存在明显的量效关系,且降压活性具有时效性;长期灌胃葵花籽ACE抑制肽,SHR体重均呈增加趋势,其中剂量组大鼠体重的增加量居于对照组和阳性对照组之间;在为期4周的长期给药试验中,除低剂量组外,其余各组均与对照组相比有显著的差异;各试验组SHR的心率值之间无显著差异性,表明葵花籽ACE抑制肽对SHR心率无显著的副作用。     

蚕蛹源ACE抑制肽的稳定性和抑制ACE动力学

研究了温度、pH、干燥方式和体外肠道酶消化对蚕蛹源ACE抑制肽稳定性的影响,并通过Lineweaver-Burk双倒数曲线作图和紫外光谱初步探讨了蚕蛹源ACE抑制肽对ACE的抑制机理。结果表明:蚕蛹源ACE抑制肽在高温、酸性和碱性条件下不稳定,易失活;冷冻干燥和喷雾干燥对蚕蛹源ACE抑制肽的活性影响较小;蚕蛹源ACE抑制肽对胃蛋白酶、胰蛋白酶和α-胰凝乳蛋白酶具有较强的抗消化能力,经胃蛋白酶、胰蛋白酶和α-胰凝乳蛋白酶共同消化后,蚕蛹源ACE抑制肽仍能保留初始活性的94.0%;蚕蛹源ACE抑制肽竞争性抑制ACE,其抑制常数(Ki)为0.06 mg/mL;ACE被蚕蛹源ACE抑制肽抑制后,ACE在240～280 nm附近的紫外吸光值明显增加,初步揭示了蚕蛹源ACE抑制肽抑制ACE活性时,ACE的分子结构发生了改变。     

葵花籽粕ACE抑制肽分离纯化及其性质研究

以葵花籽粕血管紧张素转化酶(ACE)抑制肽为原料,采用DA201-C大孔吸附树脂对其进行分离纯化,并对纯化后的葵花籽粕ACE抑制肽稳定性和活性进行了分析。结果表明:葵花籽粕ACE抑制肽最优纯化工艺为乙醇浓度70%、上样p H 5、上样流速2 BV/h、洗脱流速2 BV/h,在此条件下,得率为93.26%,纯化后的葵花籽粕ACE抑制肽的抑制率为92.23%±0.48%。葵花籽粕ACE抑制肽对热和金属离子均具有良好的稳定性,模拟体内消化实验显示其活性不受胃肠酶的影响。     

两种皮氏蛾螺ACE抑制肽的稳定性和抑制活性

通过高效反相液相色谱技术,对两种皮氏蛾螺ACE抑制肽(Ile-Val-Thr-Asn-Trp-Asp-Asp-Met-Glu-Lys(IVTNWDDMEK)和Val-Gly-Pro-Ala-Gly-Pro-Arg-Gly(VGPAGPRG)热稳定性、抗胃肠道消化吸收,抗金属离子和抗高盐、高糖的能力进行了测定。结果表明,高温100℃加热6 h,多肽的保留率下降了75%。体外模拟胃肠消化研究表明,IVTNWDDMEK和VGPAGPRG分别在胃液2 h和肠液6 h处理后,对ACE抑制率分别为30.47%、15.74%,28.01%、12.33%。金属离子Fe³⁺的添加会降低IVTNWDDMEK和VGPAGPRG的ACE抑制活性,Zn²⁺的添加会使IVTNWDDMEK的ACE抑制活性升高,使VGPAGPRG的ACE抑制活性降低,高盐高糖也会降低酶解肽的ACE抑制活性。因此,在日常生产贮存过程中,为更好的保持ACE抑制肽的稳定性,应该避免高温长时间加热、避免金属离子Fe³⁺的添加的同时降低食盐和糖的添加。     

高粱碱溶蛋白ACE抑制肽的制备及其稳定性研究

以高粱为原料,通过碱法提取制备高粱碱溶蛋白,利用不同蛋白酶对其进行酶解,结果表明Alcalase碱性蛋白酶水解高粱蛋白得到的水解产物水解度和血管紧张素转化酶(ACE)抑制率最高。在此基础上进一步考察了碱性蛋白酶酶量、pH值、温度、反应时间这4个因素对水解产物ACE抑制率的影响,并通过响应面实验优化酶解条件,得到Alcalase碱性蛋白酶水解高粱碱溶蛋白制备ACE抑制肽最优工艺为:酶解温度55.5℃,酶解时间1.68 h,pH值7.95,酶量2 360 U/g,此条件下实测ACE抑制率达到75.98%,该ACE抑制肽具有良好的热稳定性和酸碱稳定性,并且在体外经胃肠道酶系消化酶解后,依然能保持良好的抑制活性。     

ACE抑制肽研究进展

该文对目前国内外有关ACE抑制肽研究进展进行综述,重点介绍制备ACE抑制肽原料、分离提取方法、结构与活性关系、活性测定方法和功能性评价方法,并简介其在食品中应用及发展前景,以期为对ACE抑制肽进一步研究提供参考。     

ACE抑制肽的生理功能和研究进展

血管紧张素转化酶(ACE)在人体血压调节方面起着重要的生理作用.近年来天然食品来源的ACE抑制肽已成为生物活性肽研究领域的热点.ACE抑制肽通过抑制ACE活性起降血压作用.文章综述了ACE抑制肽的作用机制、结构特点、评价方法和研究进展.     

龙须菜ACE抑制肽的体外稳定性和抗氧化活性研究

以龙须菜为原料,通过酶解法制备分子量<1 kDa的龙须菜蛋白,分别以冷冻干燥和喷雾干燥收集多肽组分(GLP-F、GLP-S),研究其在体外环境的活性保留率和抗氧化能力.通过血管紧张素转化酶(AngiotensinⅠconverting enzyme,ACE)活性抑制、总抗氧化能力、DPPH·清除能力、羟自由基清除能力、...     

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human alpha s1-casein expressed in Escherichia coli.

Recombinant human alpha s1-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II, B-II and C, were isolated and their amino acid sequences identified as Tyr-Pro-Glu-Arg (residues 8-11), Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr (residues 136-143) and Asn-Asn-Val-Met-Leu-Gln-Trp (residues 164-170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132.5, 24.8 and 41.0 mumol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.     

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。     

源于食品蛋白质的血管紧张素Ⅰ转换酶抑制肽

血管紧张素I转换酶(ACE)是一种重要的血压调节因子,该酶的一些抑制剂有较好的降压效果,并作为预防和治疗高血压的食品和药物被广泛地使用。本文对不同食品来源的ACE抑制肽降压机理、结构和功能关系、应用前景进行了概述。     

酶法制备燕麦麸蛋白ACE抑制肽的研究

采用碱溶酸沉法制备了燕麦麸蛋白,并利用7种商业化蛋白酶对其进行酶解以考察生产ACE抑制肽的效果,结果表明Alcalase为最适用酶。优化了Alcalase水解燕麦麸蛋白的工艺条件,在[S]=5.0%,E/S=1.33%,pH7.5,温度60℃条件下酶解90min,酶解产物的ACE抑制活性最强(IC50=0.291mg/mL),此时水解度为11.0%,产物的相对分子质量主要集中在880Da以下。     

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion

In silico analysis of the sequences of arachin, the major storage protein of peanut suggests that it is laden with antihypertensive peptides. Physiological proteases pepsin, trypsin, chymotrypsin and pancreatin were used to release these peptides. The degree of proteolysis and in vitro angiotensin I-converting enzyme (ACE) inhibition was maximum with pepsin. The ACE inhibitor index of human gastric juice catalysed digestion was similar to pepsin demonstrating that such peptides can be produced in vivo following ingestion of arachin. Three peptides purified from the simulated gastric fluid digests were synthesized. Among them, the pentapeptide, NAQRP was the most potent with an IC₅₀ of 32 ± 2 μM. Molecular docking simulation with human tACE indicate that in addition to a favourable C-terminal Pro residue, the length of the peptides advocate ACE inhibitor potency. These results further potentiate the use of arachin/peanut proteins as functional ingredients in auxiliary therapeutic foods toward blood pressure management.     

Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir

In this study, a potent angiotensin-converting enzyme (ACE)-inhibitory activity was found in a commercial kefir made from caprine milk. The low molecular mass peptides released from caseins during fermentation were mainly responsible for this activity. Sixteen peptides were identified by HPLC-tandem mass spectrometry. Two of these peptides, with sequences PYVRYL and LVYPFTGPIPN, showed potent ACE-inhibitory properties. The impact of gastrointestinal digestion on ACE-inhibitory activity of kefir peptides was also evaluated. Some of these peptides were resistant to the incubation with pepsin followed by hydrolysis with Corolase PP. The ACE-inhibitory activity after simulated digestion was similar to or slightly lower than unhydrolyzed peptides, except for peptide β-casein f(47-52) (DKIHPF), which exhibited an activity 8 times greater after hydrolysis.     

Production,analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein

Novel angiotensin-I-converting enzyme inhibitory peptides were isolated from bovine casein hydrolysate prepared by AS1.398 neutral protease. The active hydrolysate obtained at 12 h hydrolysis showed the highest ACE-inhibitory activity and was further consecutively separated by ultrafiltration, and the 3 kDa permeate showed the highest ACE-inhibiting activity. This active fraction was further purified to yield two novel ACE-inhibiting peptides, whose amino acid sequences were Arg-Tyr-Pro-Ser-Tyr-Gly (κ-casein; f25–30) and Asp-Glu-Arg-Phe (κ-casein; f15–18), respectively. The IC₅₀ value of the peptides were 54 ± 1.2 μg/mL and 21 ± 0.8 μg/mL, respectively. The Lineweaver–Burk plots revealed that the peptides acts as a non-competitive inhibitor. Antihypertensive effect in spontaneously hypertensive rats also revealed that single and repeated oral administrations of hydrolysates of bovine casein decreased systolic blood pressure significantly in spontaneously hypertensive rats (P < 0.01, P < 0.05). These results suggested that the peptide derived from peptides from bovine casein would be a beneficial ingredient for functional food or pharmaceuticals against hypertension.