Cited by 140Protein Hydrolysis and Bioactive PeptidesSeaweed-derived Bioactive CompoundsPeptidase Inhibition and Analysis

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Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis

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Sun, Siqi, Xu, Xiaoting, Sun, Xue, Zhang, Xiaoqian, Chen, Xinping, Xu, Nianjun·2019·Marine Drugs

DOI 10.3390/md17030179PMC PMC6471128

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Abstract

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC50 values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides.

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Figure 1 Angiotensin I-converting enzyme (ACE) inhibitory activities of U. intestinalis protein hydrolysates produced by different enzymes. Each point is the mean of three determinations (n = 3) ± SD. Different letters indicate significant differences. The concentration of each hydrolysate was 2.5 mg/mL; crude protein (2.5 mg/mL) was used as the positive control.CC BY · PubMed Central

Figure 2 Effects of hydrolysis pH (A), temperature (B), substrate concentration (C), E/S ratio (D), and reaction time (E) on ACE inhibitory activity of protein hydrolysates from U. intestinalis.CC BY · PubMed Central

Figure 3 Contour plots and response surface plots for pH (A), temperature (B), and substrate concentration (C) to ACE inhibition rate.CC BY · PubMed Central

Figure 4 Sephadex G-25 gel filtration chromatogram of <3 kDa fraction of trypsin hydrolysate from U. intestinalis. (A) The fraction was divided into five parts (A–E) by Sephadex G-25. (B) The ACE inhibitory activity (1.5 mg/mL) and percentage of A–E. (C) The fraction was divided into three parts (C1–C3) by Sephadex G-15. (D) The ACE inhibitory activity (1.5 mg/mL) and percentage of C1 to C3.CC BY · PubMed Central

Figure 5 ACE inhibitory activity of fraction C2 from RP-HPLC. (A) The fraction was divided into 9 parts (C2-1 to C2-9) by RP-HPLC. (B) ACE inhibitory activity (1.5 mg/mL) and percentages of C2-1 to C2-9. Means with different lower case letters are significantly different (p < 0.05).CC BY · PubMed Central

Figure 6 The primary mass spectrogram and corresponding secondary mass spectrogram of FGMPLDR and MELVLR. (A) MS/MS spectra of FGMPLDR. (B) The secondary mass spectrogram of FGMPLDR. (C) MS/MS spectra of MELVLR. (D) The secondary mass spectrogram of MELVLR.CC BY · PubMed Central

Figure 7 Molecular docking results for FGMPLDR and MELVLR with ACE (PDB: 1O8A). (A) 3-D details of ACE and FGMPLDR interactions. (B) 2-D interaction details for FGMPLDR. (C) 3-D details of ACE and MELVLR interactions. (D) 2D interaction details for MELVLR.CC BY · PubMed Central

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“Different proteases affect the composition and size of the polypeptides produced, which can affect their biological activities [26].”
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Fitzgerald, R. J., Murray, B. A., & Walsh, D. J. (2004) · Journal of Nutrition · doi:10.1093/jn/134.4.980s · Cited by 725 · cited 1×
“captopril, and lisinopril, are widely used in hypertension treatments, synthetic ACEIs have a series of negative effects, including hypotension, cough, increased potassium levels and, angioedema [5,6].”
Background
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Ryan, J. T., Ross, R., Bolton, D., Fitzgerald, G., & Stanton, C. (2011) · Nutrients · doi:10.3390/nu3090765 · Cited by 493 · cited 2×
“According to previous studies, most ACEIPs are small peptides of 2–12 residues and molecular weights less than 3000 Da [33], which may more easily fit in the ACE active site and thus assert inhibitory activity [34].”
Background
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López‐Fandiño, R., Otte, J., & Camp, J. V. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2006.06.004 · Cited by 389 · cited 1×
“To date, ACEIPs derived from a variety of products such as milk [7], bovine collagen [8], mushrooms [9], rice [10], and marine sources including fish, shellfish, and macroalgae [11,12], have been reported.”
Background
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Wu, J., & Ding, X. (2002) · Food Research International · doi:10.1016/s0963-9969(01)00131-4 · Cited by 344 · cited 1×
“After gastrointestinal digestion, some food-derived ACEIPs do not exhibit (or exhibit fewer than) the expected hypotensive effects [38,39].”
Background
Health benefits of marine foods and ingredients
Larsen, R., Eilertsen, K., & Elvevoll, E. O. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.05.017 · Cited by 302 · cited 1×
“According to previous studies, many unique bioactive compounds, including peptides, fats, and carbohydrates, have been isolated from macroalgae [13,14].”
Background
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Sheih, I.-C., Fang, T. J., & Wu, T.-K. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2008.12.019 · Cited by 280 · cited 1×
“Proteases are necessary to release ACEIPs from inactive forms [25].”
Background
Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats
Suetsuna, K., Maekawa, K., & Chen, J.-R. (2004) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2003.11.004 · Cited by 249 · cited 1×
“5 μM), and Tyr-Asn-Lys-Leu (IC50 = 21 μM) from Undaria pinnatifida [15] and Ile-Tyr (IC50 = 2.”
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Wang, J., Hu, J., Cui, J., Bai, X., Du, Y., Miyaguchi, Y., & Lin, B. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.03.059 · Cited by 212 · cited 1×
“Hypertension seriously affects human health and is a causative factor of cardiovascular diseases, stroke, and renal diseases, among others [1,2].”
Background
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Wu, Q., Jia, J., Yan, H. H., Du, J., & Gui, Z. (2014) · Peptides · doi:10.1016/j.peptides.2014.07.026 · Cited by 193

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Chen, Q., Nie, X., Huang, W., Wang, C., Lai, R., Lu, Q., He, Q., & Yu, X. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132833 · Cited by 21
Eco-friendly nutrient from ocean: Exploring Ulva seaweed potential as a sustainable food source
Khan, N., Sudhakar, K., & Mamat, R. (2024) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2024.101239 · Cited by 33
Study on the Interaction of Algal Peptides on Virulence Factors of Helicobacter pylori: In Silico Approach
MubarakAli, D., Akshaya, T., Raghunathan, S., & Navabshan, I. (2021) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-021-03716-4 · Cited by 21
Exploration of cyclooxygenase-2 inhibitory peptides from walnut dreg proteins based on in silico and in vitro analysis
Hong, Z., Xie, J., Tao, L., Dai, J., Li, T., Zhang, L., Bai, Y., Hu, X., Chen, J., Sheng, J., et al. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2022.9250143 · Cited by 20
Study on the domain selective inhibition of angiotensin‐converting enzyme (ACE) by food‐derived tyrosine‐containing dipeptides
Song, C., Qiao, B., Zhang, Q., Wang, C., Fu, Y., & Zhu, B. (2021) · Journal of Food Biochemistry · doi:10.1111/jfbc.13779 · Cited by 20
Enhancing microalgal proteins for nutraceutical and functional food applications
Kaur, M., Bhatia, S., Bagchi, D., Tak, Y., Kaur, G., Kaur, C., Kaur, A., & Sharma, N. (2025) · Future Foods · doi:10.1016/j.fufo.2025.100564 · Cited by 19
Isolation, identification, and in vivo evaluation of the novel antihypertensive peptide, VSKRLNGDA, derived from chicken blood cells
Wongngam, W., Roytrakul, S., Mitani, T., Katayama, S., Nakamura, S., & Yongsawatdigul, J. (2022) · Process Biochemistry · doi:10.1016/j.procbio.2022.02.011 · Cited by 19
Fractionation and identification of bioactive peptides from red macroalgae protein hydrolysates: In silico analysis and in vitro bioactivities
Dhaouafi, J., Romdhani, M., Deracinois, B., Flahaut, C., Nedjar, N., & Balti, R. (2024) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2024.103211 · Cited by 18
Algae as a source of peptides inhibitors of the angiotensin-converting enzyme: a systematic review
de Amorim, A. P., SILVA, G. H. D., Costa, R. M. P. B., Porto, A. L. F., & Bezerra, R. P. (2022) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765202220201636 · Cited by 20
“With the purpose to separate the peptides based on their molecular weight, one of the methods to fractionation is the UF, which consists to separate the peptide according to its size using membrane with different cut-off (Cao et al. 2017, Sun et al. 2019).”
Method
First Report of Screening of Novel Angiotensin-I Converting Enzyme Inhibitory Peptides Derived from the Red Alga Acrochaetium sp.
Windarto, S., Lee, M., Nursyam, H., & Hsu, J. (2022) · Marine Biotechnology · doi:10.1007/s10126-022-10152-w · Cited by 20
“2018), Ulva intestinalis (Sun et al. 2019), and Pyropia pseudolinearis (Kumagai et al.”
Background
The Ocean’s Pharmacy: Health Discoveries in Marine Algae
Silva, M., Avni, D., Varela, J. C. S., & Barreira, L. A. (2024) · Molecules · doi:10.3390/molecules29081900 · Cited by 19
Marine Natural Products in Inflammation‐Related Diseases: Opportunities and Challenges
Zhang, T., Ouyang, Z., Zhang, Y., Sun, H., Kong, L., Xu, Q., Qu, J., & Sun, Y. (2025) · Medicinal Research Reviews · doi:10.1002/med.22109 · Cited by 19
Identification of novel ACE inhibitory peptides from Nannochloropsis oculata through peptidomics, in silico screening and molecular docking
Lin, L., Yuan, W., Xiao, J., Jia, J., Xie, Y., Cai, Q., Dai, C., Li, Q., & Wang, B. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.145073 · Cited by 18
Screening and Molecular Mechanisms of Novel ACE-Inhibitory Peptides from Gracilariopsis lemaneiformis
Su, Y., Chen, S., Shen, J., Yi, Z., Liu, S., Cai, S., Pan, N., Qiao, K., Chen, X., Chen, B., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314850 · Cited by 17
“isolated ACE-inhibitory peptides from the marine macroalga Ulva intestinalis by ultra-filtration, gel chromatography, and HPLC methods [16].”
MethodSelf-citation
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Dai, H., He, M., Hu, G., Li, Z., Al-Romaima, A., Wu, Z., Liu, X., & Qiu, M. (2023) · Foods · doi:10.3390/foods12183480 · Cited by 17
“Moreover, a variety of bioactive peptides obtained from the protein of marine organisms including fish [8], mollusks [9,10], seaweed [11,12], and microbial fermentation products [13,14] have been confirmed to have an ACE inhibitory function.”
Background
Noncompetitive tight‐binding inhibition of Anticarsia gemmatalis trypsins by Adenanthera pavonina protease inhibitor affects larvae survival
Meriño‐Cabrera, Y., Mendes, T. A. D. O., Castro, J. S., Barbosa, S. L., Macedo, M. L. R., & Oliveira, M. G. D. A. (2020) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21687 · Cited by 16
Complementation of reducing power for 5-hydroxyvaleric acid and 1,5-pentanediol production via glucose dehydrogenase in Escherichia coli whole-cell system
Kim, B., Oh, S. J., Hwang, J. H., Kim, H., Shin, N., Joo, J. C., Choi, K., Park, S., Park, K., Bhatia, S. K., et al. (2023) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2023.110305 · Cited by 16
Preparation, identification, activity prediction, and protective effects on IR-HepG2 cells of five novel DPP-IV inhibitory peptides from protein hydrolysate of skipjack tuna dark muscles
Meng, L., Song, Y., Zheng, B., Zhao, Y., Hong, B. S., Ma, M., Wen, Z., Miao, W., & Xu, Y. (2023) · Food & Function · doi:10.1039/d3fo02948d · Cited by 15
Targeted Affinity Purification and Mechanism of Action of Angiotensin-Converting Enzyme (ACE) Inhibitory Peptides from Sea Cucumber Gonads
Wang, Y., Chen, S., Shi, W., Liu, S., Chen, X., Pan, N., Wang, X., Su, Y., & Liu, Z. (2024) · Marine Drugs · doi:10.3390/md22020090 · Cited by 15
“Its two novel ACE inhibitors, FGMPLDR and MELVLR, which were prepared in Ulva intestinalis , also had low IC values of 219.4 µ M and 236.9 µ M, respectively [32].”
BackgroundInfluentialSelf-citation
Angiotensin-I-converting enzyme inhibitory peptides from eel (Anguilla japonica) bone collagen: preparation, identification, molecular docking, and protective function on HUVECs
Xiang, H., Huang, H., Shao, Y., Hao, S., Li, L., Wei, Y., Chen, S., & Zhao, Y. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1462656 · Cited by 15
Marine-derived protein: peptide bioresources for the development of nutraceuticals for improved athletic performance
Penggalih, M. H. S. T., Praditya, G. N., Rizqiansyah, C. Y., Setyawardani, A., Purnomo, A. F., Maulana, R. A., Gunawan, W. B., Subali, D., Kurniawan, R., Mayulu, N., et al. (2023) · Frontiers in Sports and Active Living · doi:10.3389/fspor.2023.1281397 · Cited by 14
Pharmacoinformatics and cellular studies of algal peptides as functional molecules to modulate type-2 diabetes markers
Kurniawan, R., Taslim, N. A., Hardinsyah, H., Syauki, A. Y., Idris, I., Aman, A. M., Permatasari, H. K., Wiyarta, E., Surya, R., Mayulu, N., et al. (2024) · Future Foods · doi:10.1016/j.fufo.2024.100354 · Cited by 14
Moringa leaf extract and green algae improve the growth and physiological attributes of Mentha species under salt stress
Al-Taisan, W. A., Alabdallah, N. M., & Almuqadam, L. (2022) · Scientific Reports · doi:10.1038/s41598-022-18481-5 · Cited by 14
Concentration and purification of seaweed extracts using membrane technologies
Díaz-Reinoso, B. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817943-7.00014-7 · Cited by 14
In vitro enzyme inhibitory effects of green and brown Australian seaweeds and potential impact on metabolic syndrome
Shannon, E., Conlon, M. A., & Hayes, M. (2023) · Journal of Applied Phycology · doi:10.1007/s10811-022-02900-1 · Cited by 12
Molecular binding mechanism and novel antidiabetic and anti-hypertensive bioactive peptides from fermented camel milk with anti-inflammatory activity in raw macrophages cell lines
Shukla, P., Sakure, A. A., Basaiawmoit, B., Khakhariya, R., Maurya, R., Bishnoi, M., Kondepudi, K. K., Liu, Z., Padhi, S., Rai, A. K., et al. (2023) · Amino Acids · doi:10.1007/s00726-023-03335-9 · Cited by 12
“Sun et al. (2019) investigated the peptides with molecular weights below 3 kDa can effectively stop the ACE activity.”
Background
Alaria esculenta, Ulva lactuca, and Palmaria palmata as Potential Functional Food Ingredients for the Management of Metabolic Syndrome
Shannon, E., & Hayes, M. (2025) · Foods · doi:10.3390/foods14020284 · Cited by 12
“Other mechanisms have been attributed to zinc and hydrogen bond interactions [16].”
Molecular modeling in cardiovascular pharmacology: Current state of the art and perspectives
Lagoutte‐Renosi, J., Allemand, F., Ramseyer, C., Yesylevskyy, S. O., & Davani, S. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.026 · Cited by 12
Purification, Identification, and In Silico Analysis of Anti-Obesity and Antidiabetic Peptides from the Red Seaweed Palmaria palmata
Ghelichi, S., Hajfathalian, M., Helalat, S. H., Svensson, B., & Jacobsen, C. (2025) · Marine Drugs · doi:10.3390/md23100392 · Cited by 13
“Several studies have supported its use for producing protein hydrolysates with high yields and desirable functional properties from various seaweed biomasses [24–27].”
Angiotensin-I converting enzyme (ACE) inhibitory bioaccessible peptides obtained from protein extracts of Macrocystis pyrifera and Chondracanthus chamissoi seaweeds
Vásquez, V., Martínez, R., Rodríguez-Núñez, K., & Bernal, C. (2024) · Algal Research · doi:10.1016/j.algal.2024.103575 · Cited by 10
Advances in analytical techniques coupled to in vitro bioassays in the search for new peptides with functional activity in effect-directed analysis
Guerra-Fajardo, L. D., Pavón-Pérez, J., Vallejos‐Almirall, A., & Jorquera-Pereira, D. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.133784 · Cited by 11
Hydrolysate protein from brown macroalgae ( Sargassum ilicifolium ): Antioxidant, antitumor, antibacterial, and ACE inhibitory activities
Mousaie, M., Khodadadi, M., & Tadayoni, M. (2022) · Journal of Food Processing and Preservation · doi:10.1111/jfpp.17020 · Cited by 10
The Molecular Docking and Inhibition Kinetics of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Soft-Shelled Turtle Yolk
Nong, N. T. P., Sutopo, C. C. Y., Hung, W., Wu, P., & Hsu, J. (2022) · Applied Sciences · doi:10.3390/app122312340 · Cited by 10
Ameliorative effect of mussel-derived ACE inhibitory peptides on spontaneous hypertension rats
You, Q., Sun, X., Chen, J., Yu, J., & Wei, Y. (2023) · European Journal of Nutrition · doi:10.1007/s00394-023-03222-9 · Cited by 10
Self-citation
Characterization of Proteins Extracted from Ulva sp., Padina sp., and Laurencia sp. Macroalgae Using Green Technology: Effect of In Vitro Digestion on Antioxidant and ACE-I Inhibitory Activity
Şensu, E., Ayar, E. N., Okudan, E. Ş., Özçelik, B., & Yücetepe, A. (2023) · ACS Omega · doi:10.1021/acsomega.3c05041 · Cited by 10
Purification of angiotensin converting enzyme inhibitory peptides and antihypertensive effect generated from Indonesian traditional fermented beef (Cangkuk)
Mirdhayati, I., Zain, W. N. H., Fatah, A., Yokoyama, I., & Arihara, K. (2024) · Animal Bioscience · doi:10.5713/ab.23.0433 · Cited by 10
“Factors determining ACE-inhibitory activity are amino acid composition, propensity to bind hydrophobic amino acids, small peptides, and molecular weights 3,000 Da [24].”
Background
Valorization of Hakka Huangjiu lees: Optimization of ultrasound-assisted enzymatic extraction and identification of angiotensin I-converting enzyme inhibitory peptides
Yang, S., Wang, H., Bai, W., Zhao, W., Liu, G., & Liu, X. (2024) · Food and Bioproducts Processing · doi:10.1016/j.fbp.2024.05.010 · Cited by 9
Abalone Viscera Fermented with Aspergillus oryzae 001 Prevents Pressure Elevation by Inhibiting Angiotensin Converting Enzyme
Iwamoto, N., Sasaki, A., Maizawa, T., & Hamada‐Sato, N. (2023) · Nutrients · doi:10.3390/nu15040947 · Cited by 9
Bioactive peptide production and determination of functional properties using crude water extracts of Ulva lactuca (Chlorophyta) and Sargassum crassifolium (Phaeophyceae) collected from Sri Lanka
Hamit, C. S., Nam, K., & Abeyrathne, E. D. N. S. (2022) · Applied Phycology · doi:10.1080/26388081.2022.2063758 · Cited by 9
“…antihypertensive, anticoagulant, anti-diabetic, and anti-HIV, depending on their structural properties (Admassu et al., 2018; Bondu et al., 2015; Cian, Garzón, Ancona, Guerrero, & Drago, 2016; Harnedy & FitzGerald, 2011, 2013; Sarmadi & Ismail, 2010; Sun et al., 2019; tePimentel et al., 2019).”
Synergistic Effect of Surfactant on Disperser Energy and Liquefaction Potential of Macroalgae (Ulva intestinalis) for Biofuel Production
Veettil, R. P., Rabia, R., Kumar, M. D., Gondi, R., Sankarapandian, K., Kannan, M., Kumar, G., Al-Qaradawi, S. Y., & Jeyakumar, R. B. (2023) · Fermentation · doi:10.3390/fermentation9010055 · Cited by 9
Neuroprotective peptides isolated from flavourzyme-pea protein hydrolysate protect human SH-SY5Y cells from Aβ1-42 induced apoptosis
Hsieh, L., Hsu, Y.-C., & Chiang, W. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105755 · Cited by 8
GRU4ACE : Enhancing ACE inhibitory peptide prediction by integrating gated recurrent unit with multi‐source feature embeddings
Ahmad, S., Schaduangrat, N., Chumnanpuen, P., & Shoombuatong, W. (2025) · Protein Science · doi:10.1002/pro.70026 · Cited by 9
“Similarly, glutamic acid (E) shows a marked contrast, being present in 5.35% of active peptides versus only 1.15% in inactive ones, underscoring its beneficial effect on inhibitory activity (Sun et al., 2019; Wang et al., 2021).”
Influential
Identification of Novel Nonapeptides from Sipunculus nudus L. and Comparing Its ACEI Activities Mechanism by Molecular Docking
Qi, Y., Tang, X., Liu, H., Lin, Q., Lu, Y., & Luo, H. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10328-3 · Cited by 8
A Perspective on Enzyme Inhibitors from Marine Organisms
Tischler, D. (2020) · Marine Drugs · doi:10.3390/md18090431 · Cited by 8
“For example, the algae Ulva intestinalis was used to generate a protein hydrolysate containing potential bioactives [11].”
Method
Nanoliposomal Encapsulation and Purification of Angiotensin-Converting Enzyme Inhibitor Peptides from Ulva rigida
Şensu, E., Koku, H., Demircan, E., Şişman, S., Gülseren, İ., Karaduman, T., Çakır, B., Okudan, E. Ş., Duruksu, G., Özçelik, B., et al. (2025) · ACS Omega · doi:10.1021/acsomega.5c00780 · Cited by 7
Green Seaweeds as a Potential Source of Biomolecules and Bioactive Peptides: Recent Progress and Applications – A Review
Das, S., Behera, M., Das, S. R., Behera, K. C., & Singh, L. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202401695 · Cited by 7
Antioxidant, antidiabetic, and antihypertensive activities of defatted pigmented rice bran protein hydrolysates
Mojumder, M. N., Mahmud, Z., Khan, I. M., Tamanna, S., Rahman, M. A., Ferdous, N., Alauddin, M., & Howlader, M. Z. H. (2024) · Discover Applied Sciences · doi:10.1007/s42452-024-06304-3 · Cited by 7
“[58].”

Authors: Sun, S., Xu, X., Sun, X., Zhang, X., Chen, X., & Xu, N.
Affiliations: Ningbo University (CN)
Vanderbilt University Medical Center (US)
Corresponding author: Xu, Nianjun
ORCID: Sun, Siqi
Sun, Xue
Zhang, Xiaoqian
Chen, Xinping
Xu, Nianjun
Venue: Marine Drugs
Publisher: MDPI AG
Published: 2019-03-19
Volume: 17
Issue: 3
Pages: 179
ISSN: 1660-3397 (ISSN-L)
DOI: 10.3390/md17030179
PMC: PMC6471128
OpenAlex: W2922600776
Cited by: 140
References: 50
Citations by year: 2026: 9 · 2025: 21 · 2024: 29 · 2023: 22 · 2022: 27 · 2021: 15 · 2020: 14 · 2019: 3
FWCI: 4.88
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Marine Drugs (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Discover Archive (Vanderbilt University) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: Natural Science Foundation of Zhejiang Province (LZ17D060001)
Ningbo International Cooperation Program (2017D10019)
Ningbo Municipal Bureau of Science and Technology (2016C10034)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Keywords: ACE inhibitory peptides, Ulva intestinalis, seaweed, protein hydrolysates, trypsin hydrolysis, enzymatic hydrolysis optimization, peptide purification, antihypertensive peptides, food-derived bioactive peptides, zinc binding
MeSH terms: Angiotensin-Converting Enzyme Inhibitors, Antihypertensive Agents, Drug Stability, Hydrolysis, Hypertension, Peptidyl-Dipeptidase A, Peptide Hydrolases, Peptides, Protein Hydrolysates, Seaweed, Inhibitory Concentration 50, Ulva, Enzyme Assays, Molecular Docking Simulation

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Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis

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