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1.
We examined the inhibitory activity of angiotensin I converting enzyme (ACE) in protein hydrolysates from dulse, Palmaria palmata. The proteins extracted from dulse were mainly composed of phycoerythrin (PE) followed by phycocyanin (PC) and allophycocyanin (APC). The dulse proteins showed slight ACE inhibitory activity, whereas the inhibitory activity was extremely enhanced by thermolysin hydrolysis. The ACE inhibitory activity of hydrolysates was hardly affected by additional pepsin, trypsin and chymotrypsin treatments. Nine ACE inhibitory peptides (YRD, AGGEY, VYRT, VDHY, IKGHY, LKNPG, LDY, LRY, FEQDWAS) were isolated from the hydrolysates by reversed-phase high-performance liquid chromatography (HPLC), and it was demonstrated that the synthetic peptide LRY (IC50: 0.044 μmol) has remarkably high ACE inhibitory activity. Then, we investigated the structural properties of dulse phycobiliproteins to discuss the origin of dulse ACE inhibitory peptides. Each dulse phycobiliprotein possesses α-subunit (Mw: 17,477–17,638) and β-subunit (Mw: 17,455–18,407). The sequences of YRD, AGGEY, VYRT, VDHY, LKNPG and LDY were detected in the primary structure of PE α-subunit, and the LDY also exists in the APC α- and β-subunits. In addition, the LRY sequence was found in the β-subunits of PE, PC and APC. From these results, it was suggested that the dulse ACE inhibitory peptides were derived from phycobiliproteins, especially PE. To make sure the deduction, we carried out additional experiment by using recombinant PE. We expressed the recombinant α- and β-subunits of PE (rPEα and rPEβ, respectively), and then prepared their peptides by thermolysin hydrolysis. As a result, these peptides showed high ACE inhibitory activities (rPEα: 94.4%; rPEβ: 87.0%). Therefore, we concluded that the original proteins of dulse ACE inhibitory peptides were phycobiliproteins.  相似文献   

2.
分别以碱性蛋白酶Alcalase和中性蛋白酶Neutrase对花生分离蛋白进行水解．制备花生分离蛋白水解物．并测定不同水解时间所得产物对血管紧张素转化酶(ACE)的抑制活性。未水解的花生分离蛋白没有ACE抑制活性．用中性蛋白酶Neutrase水解所得的水解物显示弱ACE抑制活性。然而，碱性蛋白酶Alcalasc水解物具有很强的ACE抑制活性．水解0．5h时水解物活性最高，其半抑制浓度为(IC50)0．56mg／mL。本研究表明，当用碱性蛋白酶Alcalase水解时，花生分离蛋白是生产ACE抑制肽的良好蛋白质来源，花生分离蛋白碱性蛋白酶Alcalase水解物可作为具有降压功能的功能食品添料。  相似文献   

3.
Food-derived bioactive compounds are gaining increasing significance in life sciences. In the present study, we identified angiotensin I-converting enzyme (ACE)-inhibitory peptides from Mactra veneriformis hydrolysate using a nano-LC-MS/MS method. Mactra veneriformis hydrolysate was first separated into four fractions (F1–F4) based on molecular weight by ultrafiltration. The fraction with molecular weight lower than 1 kDa (F1) showed the highest ACE inhibitory activity. F1 was then analyzed by a high throughput nano-LC-MS/MS method and sequences of peptides in F1 were calculated accordingly. The 27 peptides identified as above were chemically synthesized and tested for ACE-inhibitory activity. The hexapeptide VVCVPW showed the highest potency with an IC50 value of 4.07 μM. We then investigated the interaction mechanism between the six most potent peptides and ACE by molecular docking. Our docking results suggested that the ACE inhibitory peptides bind to ACE via interactions with His383, His387, and Glu411 residues. Particularly, similar to the thiol group of captopril, the cysteine thiol group of the most potent peptide VVCVPW may play a key role in the binding of this peptide to the ACE active site.  相似文献   

4.
The study aimed to characterize and identify anti-diabetic and anti-hypertensive bioactive peptides generated upon enzymatic hydrolysis of quinoa protein isolates. Different quinoa protein hydrolysates (QPHs) were produced using food grade enzymes like Bromelain, chymotrypsin and Pronase E at a hydrolysis interval of 2 h up to 6 h. QPHs were characterized for their physicochemical properties using degree of hydrolysis, SDS-PAGE, and their anti-diabetic properties via inhibition of dipeptidyl peptidase-IV (DPP-IV) and α-glucosidase (AG), and anti-hypertensive property via inhibition of angiotensin converting enzyme (ACE) were explored. IC50 for DPP-IV, AG and ACE inhibitory activities of QPHs were in the range of 0.72–1.12, 1.00–1.86 and 0.18–0.31 mg/mL, respectively. The chymotrypsin derived 6 h hydrolysate (QC6) was sequenced for peptides identification and 136 peptides were identified among which 35 peptides were predicted as potential bio-active peptides (BAPs) based on their Peptide Ranker score. Results showed that identified peptides were predicted to possess high potential in inhibiting the DPP-IV, AG and ACE. In particular, QHPHGLGALCAAPPST was found to bind to the highest number of active hotspots of the target enzymes that are involved in their enzymatic activities. In conclusion, quinoa protein hydrolysates were identified as potential sources of BAPs with inhibitory properties towards key enzymes involved in the control of type 2 diabetes and hypertension.  相似文献   

5.
The aim of this work was the purification and identification of the major angiotensin converting enzyme (ACE) inhibitory peptides produced by enzymatic hydrolysis of a protein concentrate recovered from a cuttlefish industrial manufacturing effluent. This process consisted on the ultrafiltration of cuttlefish softening wastewater, with a 10 kDa cut-off membrane, followed by the hydrolysis with alcalase of the retained fraction. Alcalase produced ACE inhibitors reaching the highest activity (IC50 = 76.8 ± 15.2 μg mL−1) after 8 h of proteolysis. Sequential ultrafiltration of the 8 h hydrolysate with molecular weight cut-off (MWCO) membranes of 10 and 1 kDa resulted in the increased activity of each permeate, with a final IC50 value of 58.4 ± 4.6 μg mL−1. Permeate containing peptides lower than 1 kDa was separated by reversed-phase high performance liquid chromatography (RP-HPLC). Four fractions (A–D) with potent ACE inhibitory activity were isolated and their main peptides identified using high performance liquid chromatography coupled to an electrospray ion trap Fourier transform ion cyclotron resonance-mass spectrometer (HPLC-ESI-IT-FTICR) followed by comparison with databases and de novo sequencing. The amino acid sequences of the identified peptides contained at least one hydrophobic and/or a proline together with positively charged residues in at least one of the three C-terminal positions. The IC50 values of the fractions ranged from 1.92 to 8.83 μg mL−1, however this study fails to identify which of these peptides are ultimately responsible for the potent antihypertensive activity of these fractions.  相似文献   

6.
Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from marine organism have shown a blood pressure lowering effect with no side effects. A new affinity medium of Fe3O4@ZIF-90 immobilized ACE (Fe3O4@ZIF-90-ACE) was prepared and used in the purification of ACE inhibitory peptides from Wakame (Undaria pinnatifida) protein hydrolysate (<5 kDa). The Fe3O4@ZIF-90 nanoparticles were prepared by a one-pot synthesis and crude ACE extract from pig lung was immobilized onto it, which exhibited excellent stability and reusability. A novel ACE inhibitory peptide, KNFL (inhibitory concentration 50, IC50 = 225.87 μM) was identified by affinity purification using Fe3O4@ZIF-90-ACE combined with reverse phase-high performance liquid chromatography (RP-HPLC) and MALDI-TOF mass spectrometry. Lineweaver–Burk analysis confirmed the non-competitive inhibition pattern of KNFL, and molecular docking showed that it bound at a non-active site of ACE via hydrogen bonds. This demonstrates that affinity purification using Fe3O4@ZIF-90-ACE is a highly efficient method for separating ACE inhibitory peptides from complex protein mixtures and the purified peptide KNFL could be developed as a functional food ingredients against hypertension.  相似文献   

7.
The present study was carried out to characterize ACE inhibitory peptides which are released from the trypsin hydrolysate of wheat gluten protein. In silico proteolitic digestion of a high molecular weight glutenin subunit was performed. Among the resultant fragments, four peptides were selected for chemical synthesis based on the chemoinformatics studies and docking properties. The ACE inhibitory activity and kinetic parameters of the most important peptides were determined. Molecular docking simulation was also performed to predict the sites on ACE in which these peptides bind and displayed inhibition mechanisms. Two peptide sequences of IPALLKR (P4) and AQQLAAQLPAMCR (P6) showed higher ACE inhibitory activity among peptide collection. The IC50 values of P6 and P4 were 43 ± 1.3 μM and 68 ± 2.8 μM, respectively. P6 peptide was proved to be a more potent ACE inhibitor than P4 peptide. Lineweaver-Burk plots revealed that P6 and P4 behaved as non-competitive and competitive ACE inhibitors, respectively. The simulations showed that P4 bound to the active site region. Conversely, P6 bound to the N-terminus entrance of substrate tunnel and obstructed the substrate access into the catalytic site. Overall, the results showed that these peptides would be considered as a model for discovering new bio-compatible ACE inhibitors.  相似文献   

8.
Fish discards and by-products can be transformed into high value-added products such as fish protein hydrolysates (FPH) containing bioactive peptides. Protein hydrolysates were prepared from different parts (whole fish, skin and head) of several discarded species of the North-West Spain fishing fleet using Alcalase. All hydrolysates had moisture and ash contents lower than 10% and 15%, respectively. The fat content of FPH varied between 1.5% and 9.4% and had high protein content (69.8–76.6%). The amino acids profiles of FPH are quite similar and the most abundant amino acids were glutamic and aspartic acids. All FPH exhibited antioxidant activity and those obtained from Atlantic horse mackerel heads presented the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, reducing power and Cu2+ chelating activity. On the other hand, hydrolysates from gurnard heads showed the highest ABTS radical scavenging activity and Fe2+ chelating activity. In what concerns the α-amylase inhibitory activity, the IC50 values recorded for FPH ranged between 5.70 and 84.37 mg/mL for blue whiting heads and whole Atlantic horse mackerel, respectively. α-Glucosidase inhibitory activity of FPH was relatively low but all FPH had high Angiotensin Converting Enzyme (ACE) inhibitory activity. Considering the biological activities, these FPH are potential natural additives for functional foods or nutraceuticals.  相似文献   

9.
The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe914 (contained in the XO) in the XO inhibitory activity of the peptides.  相似文献   

10.
Gluten hydrolysates were prepared by limited enzymatic hydrolysis with a protease having a chymotryptic activity in the presence or in the absence of cysteine during the dispersion phase of the process. The hydrolysates were fractionated by ultrafiltration, using two inorganic membranes with different molecular weight cut-off (MWCO), 50 kg/mol and 150 kg/mol. The retentates were enriched in hydrophobic peptides and the permeates were enriched in hydrophilic peptides. The foaming and emulsifying properties of hydrolysates, retentates and permeates were analysed at two pHs (4 and 6·5) and two salt concentrations (0·2 and 2% NaCl). Hydrolysates displayed a foaming capacity, but the foams were not stable. Permeates generated foams at pH 6·5 only, and these foams had a very short life-time. Permeates displayed no emulsifying properties. Retentates yielded foams with a good stability and were more efficient than whole hydrolysates to stabilise emulsions. They provided a strong resistance to coalescence. The functional properties of retentates were only sightly influenced by pH and ionic strength. Neither cysteine addition, which helps gluten dispersion and increases the yield of soluble hydrolysate, nor the MWCO of the ultrafiltration membranes influenced the functionality of the hydrolysate fractions.  相似文献   

11.
Immature rice was reported to contain higher quantities of bioactive compounds than mature rice. Young rice protein is easy to digest and has hypoallergenic potential, with protein content of 7.2–11.5% compared to rice bran at 9.8%. Few studies have reported on bioactivities and characterization of young rice proteins and their hydrolysates. Bioactivities of native protein and protein hydrolysates of two rice varieties (white rice and colored rice) were characterized and investigated for four development stages (flowery, milky, dough, and mature). Degree of hydrolysis of young rice protein was considerably higher than at the mature stage. Highest DPPH and iron chelating activity were found in alcalase® protein hydrolysate during the flowery-to-milky stage. Iron chelating activity was constant in all development stages because of the low polar amino acid content in rice. The ACE activity of alcalase® protein hydrolysate was higher than native protein at the same development stage, as observed in the milky and dough stages. Inhibitory activity of young rice hydrolysate HepG2 cells was concentration-dependent and not correlated with protein molecular size.  相似文献   

12.
In previous studies, it has not been reported that protein isolated from chia interferes favorably with antibacterial activity, and reduces cholesterol synthesis. The objective of this study was to determine whether commonly used commercial microbial proteases can be utilized to generate chia protein-based antibacterial and hypocholesterolemic hydrolysates/peptides, considering the effects of protein extraction method. Alcalase, Flavourzyme and sequential Alcalase-Flavourzyme were used to produce hydrolysates from chia protein (CF), protein-rich fraction (PRF) and chia protein concentrates (CPC1 and CPC2). These hydrolysates were evaluated for their antimicrobial activity against Gram-positive (G+) and Gram-negative (G?) microorganisms. The protein hydrolysates were purified by ultrafiltration through a membrane with 3 kDa nominal molecular weight, for evaluation of hypocholesterolemic activity. An inhibition zone was observed when the hydrolysate was tested against S. aureus, and minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC) values were obtained. Peptides from chia protein with molecular mass lower than 3 kDa reduced up to 80.7% of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) enzymatic reaction velocity. It was also observed that, independent of the method used to obtain chia proteins, the fractions showed relevant bioactivity. Moreover, the intensity of the bioactivity varied with the method for obtaining the protein and with the enzyme used in the hydrolysis process. This is the first report to demonstrate that chia peptides are able to inhibit cholesterol homeostasis.  相似文献   

13.
为考察醋制对黑豆蛋白含量及多肽ACE抑制活性的影响,为对黑豆醋浸过程中蛋白组分及含量变化进行分析,并对相应ACE抑制肽活性进行测定。黑豆经醋浸不同时间后,采用顺序抽提法提取清蛋白、球蛋白、醇溶蛋白和谷蛋白,并采用凯氏定氮法及SDS-PAGE电泳进行定量和定性分析;各蛋白组分经胃蛋白酶水解,经超滤(截留分子量3 k D)后收集滤液,获得多肽组分,RP-HPLC法进行ACE抑制活性评价。结果表明:经醋浸14 d后,黑豆总蛋白含量变化幅度小于±0.5%;清蛋白含量由55.13%(0 d)降低至9.61%(14 d);球蛋白由7.04%(0 d)增加到20.34%(14 d);醇溶蛋白由0.81%(0 d)增加到1.72(14 d);谷蛋白由21.11%(0 d)增加到59.45%(14 d),含量最高。醋浸处理降低了清蛋白源多肽的ACE抑制活性,但提高了球蛋白、醇溶蛋白及谷蛋白多肽的ACE抑制活性,其中,谷蛋白多肽抑制率由18.18%(0 d)增加至37.58%(14 d),抑制活性升高。醋浸可改变黑豆各蛋白组分的含量和对应多肽的ACE抑制活性,其中,谷蛋白含量及其多肽ACE抑制活性均有增加。研究结果表明可进一步采用分离纯化技术从谷蛋白多肽中获得高活性降压肽。  相似文献   

14.
Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (<1, 1–3, 3–10, 10–50, and >50 kDa). The components with MWs < 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC–MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L−1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.  相似文献   

15.
Plant protein hydrolysates are a source of bioactive peptides. There are peptides that decrease the micellar cholesterol solubility from bile acids and therefore may reduce in vivo cholesterol absorption. The presence of these peptides in sunflower protein hydrolysates has been studied. Sunflower protein hydrolysates produced with alcalase plus flavourzyme or with pepsin plus pancreatin inhibited in some degree the cholesterol incorporation to micelles. Protein hydrolysates generated after 30 min of hydrolysis with alcalase, and after 30 min of hydrolysis with pepsin, were the inhibitoriest of the cholesterol incorporation to micelles. The average amino acid hydrophobicity of inhibitory peptides in cholesterol micelles was higher than the observed in the corresponding protein hydrolysates. This high hydrophobicity probably favours their inclusion in the lipid micelles. In vivo, this inhibition may translate in a decrease of cholesterol absorption. Reported results show that a combination of different characteristics such as peptide size or hydrophobicity may be responsible of the inhibitory activity of generated peptides.  相似文献   

16.
Coix seed, which is a traditional Chinese medicine, has been used to treat hypertension for thousands of years. It has been shown that Coix prolamin peptides display high levels of angiotensin I converting enzyme (ACE) inhibitory activity. Hence, we purified the ACE inhibitory peptides from Coix prolamin hydrolysates and evaluated the influence of the most potent peptide on the renin-angiotensin system (RAS) genes expression in human umbilical vein endothelial cells (HUVECs). In this study, Coix prolamin peptides were sequentially separated by ultrafiltration, ion exchange chromatography, gel filtration chromatography and RP-HPLC, while the peptide structure was analyzed by mass spectrometry. Next, in silico proteolysis, pharmacophore and molecular docking were further applied to screen and optimize the structure of peptides. Finally, a novel ACE inhibitory peptide VDMF was obtained, in which its influence on the gene expression of RAS signaling pathway in AngⅡ-injury HUVECs was evaluated by quantitative real-time PCR. VDMF significantly down-regulated ACE, AngII type 1 receptor (AT1R) and ACE2 mRNA expression in comparation with model group, while up-regulating Mas gene expression. Hence, we obtained a novel antihypertensive candidate that was derived from the Coix peptides, which could involve a multi-modulation mechanism that regulates blood pressure.  相似文献   

17.
The antinociceptive and anti-inflammatory activity of caulerpin was investigated. This bisindole alkaloid was isolated from the lipoid extract of Caulerpa racemosa and its structure was identified by spectroscopic methods, including IR and NMR techniques. The pharmacological assays used were the writhing and the hot plate tests, the formalin-induced pain, the capsaicin-induced ear edema and the carrageenan-induced peritonitis. Caulerpin was given orally at a concentration of 100 μmol/kg. In the abdominal constriction test caulerpin showed reduction in the acetic acid-induced nociception at 0.0945 μmol (0.0103–1.0984) and for dypirone it was 0.0426 μmol (0.0092–0.1972). In the hot plate test in vivo the inhibition of nociception by caulerpin (100 μmol/kg, p.o.) was also favorable. This result suggests that this compound exhibits a central activity, without changing the motor activity (seen in the rotarod test). Caulerpin (100 μmol/kg, p.o.) reduced the formalin effects in both phases by 35.4% and 45.6%, respectively. The possible anti-inflammatory activity observed in the second phase in the formalin test of caulerpin (100 μmol/kg, p.o.) was confirmed on the capsaicin-induced ear edema model, where an inhibition of 55.8% was presented. Indeed, it was also observed in the carrageenan-induced peritonitis that caulerpin (100 μmol/kg, p.o.) exhibited anti-inflammatory activity, reducing significantly the number of recruit cells by 48.3%. Pharmacological studies are continuing in order to characterize the mechanism(s) responsible for the antinociceptive and anti-inflammatory actions and also to identify other active principles present in Caulerpa racemosa.  相似文献   

18.
Angiotensin-I-converting enzyme (ACE) is a crucial enzyme or receptor that catalyzes the generation of potent vasopressor angiotensin II (Ang II). ACE inhibitory peptides from fish showed effective ACE inhibitory activity. In this study, we reported an ACE inhibitory peptide from Takifugu bimaculatus (T. bimaculatus), which was obtained by molecular docking with acid-soluble collagen (ASC) hydrolysate of T. bimaculatus. The antihypertensive effects and potential mechanism were conducted using Ang-II-induced human umbilical vein endothelial cells (HUVECs) as a model. The results showed that FNLRMQ alleviated the viability and facilitated apoptosis of Ang-II-induced HUVECs. Further research suggested that FNLRMQ may protect Ang-II-induced endothelial injury by regulating Nrf2/HO-1 and PI3K/Akt/eNOS signaling pathways. This study, herein, reveals that collagen peptide FNLRMQ could be used as a potential candidate compound for antihypertensive treatment, and could provide scientific evidence for the high-value utilization of marine resources including T. bimaculatus.  相似文献   

19.
In this study, the stable collagen hydrolysate was prepared by alcalase hydrolysis and twice simulated gastrointestinal digestion from Alaska pollock skin. The characteristics of hydrolysates and antioxidant activities in vitro, including 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) radical (ABTS•+) scavenging activity, ferric-reducing antioxidant power (FRAP) and hydroxyl radical (OH·) scavenging activity, were determined. After twice simulated gastrointestinal digestion of skin collagen (SGI-2), the degree of hydrolysis (DH) reached 26.17%. The main molecular weight fractions of SGI-2 were 1026.26 and 640.53 Da, accounting for 59.49% and 18.34%, respectively. Amino acid composition analysis showed that SGI-2 had high content of total hydrophobic amino acid (307.98/1000). With the simulated gastrointestinal digestion progressing, the antioxidant activities increased significantly (p < 0.05). SGI-2 was further purified by gel filtration chromatography, ion exchange chromatography and high performance liquid chromatography, and the A1a3c–p fraction with high hydroxyl radical scavenging activity (IC50 = 7.63 μg/mL) was obtained. The molecular weights and amino acid sequences of key peptides of A1a3c–p were analyzed using high resolution mass spectrometry (LC-ESI-LTQ-Orbitrap-MS) combined with de novo software and UniProt of MaxQuant software. Four peptides were identified from A1a3c–p, including YGCC (444.1137 Da) and DSSCSG (554.1642 Da) identified by de novo software and NNAEYYK (900.3978 Da) and PAGNVR (612.3344 Da) identified by UniProt of MaxQuant software. The molecular weights and amino acid sequences of four peptides were in accordance with the features of antioxidant peptides. The results indicated that different peptides were identified by different data analysis software according to spectrometry mass data. Considering the complexity of LC-ESI-LTQ-Orbitrap-MS, it was necessary to use the different methods to identify the key peptides from protein hydrolysates.  相似文献   

20.
To prepare bioactive peptides with high angiotensin-I-converting enzyme (ACE)-inhibitory (ACEi) activity, Alcalase was selected from five kinds of protease for hydrolyzing Skipjack tuna (Katsuwonus pelamis) muscle, and its best hydrolysis conditions were optimized using single factor and response surface experiments. Then, the high ACEi protein hydrolysate (TMPH) of skipjack tuna muscle was prepared using Alcalase under the optimum conditions of enzyme dose 2.3%, enzymolysis temperature 56.2 °C, and pH 9.4, and its ACEi activity reached 72.71% at 1.0 mg/mL. Subsequently, six novel ACEi peptides were prepared from TMPH using ultrafiltration and chromatography methods and were identified as Ser-Pro (SP), Val-Asp-Arg-Tyr-Phe (VDRYF), Val-His-Gly-Val-Val (VHGVV), Tyr-Glu (YE), Phe-Glu-Met (FEM), and Phe-Trp-Arg-Val (FWRV), with molecular weights of 202.3, 698.9, 509.7, 310.4, 425.6, and 606.8 Da, respectively. SP and VDRYF displayed noticeable ACEi activity, with IC50 values of 0.06 ± 0.01 and 0.28 ± 0.03 mg/mL, respectively. Molecular docking analysis illustrated that the high ACEi activity of SP and VDRYF was attributed to effective interaction with the active sites/pockets of ACE by hydrogen bonding, electrostatic force, and hydrophobic interaction. Furthermore, SP and VDRYF could significantly up-regulate nitric oxide (NO) production and down-regulate endothelin-1 (ET-1) secretion in HUVECs after 24 h treatment, but also abolish the negative effect of 0.5 μM norepinephrine (NE) on the generation of NO and ET-1. Therefore, ACEi peptides derived from skipjack tuna (K. pelamis) muscle, especially SP and VDRYF, are beneficial components for functional food against hypertension and cardiovascular diseases.  相似文献   

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